A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
Established cell cultures that have the potential to propagate indefinitely.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
An eph family receptor that is found primarily in adult BRAIN and variety of tissues in the developing embryo tissues. During embryonic development high levels of EphA3 receptor expression is seen in the nervous system and coincides with neuronal cell migration, suggesting a role for this protein in axonal pathfinding.
An electrophysiologic technique for studying cells, cell membranes, and occasionally isolated organelles. All patch-clamp methods rely on a very high-resistance seal between a micropipette and a membrane; the seal is usually attained by gentle suction. The four most common variants include on-cell patch, inside-out patch, outside-out patch, and whole-cell clamp. Patch-clamp methods are commonly used to voltage clamp, that is control the voltage across the membrane and measure current flow, but current-clamp methods, in which the current is controlled and the voltage is measured, are also used.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Proteins prepared by recombinant DNA technology.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The opening and closing of ion channels due to a stimulus. The stimulus can be a change in membrane potential (voltage-gated), drugs or chemical transmitters (ligand-gated), or a mechanical deformation. Gating is thought to involve conformational changes of the ion channel which alters selective permeability.
A subgroup of TRP cation channels that contain 3-4 ANKYRIN REPEAT DOMAINS and a conserved C-terminal domain. Members are highly expressed in the CENTRAL NERVOUS SYSTEM. Selectivity for calcium over sodium ranges from 0.5 to 10.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
Regulatory proteins that down-regulate phosphorylated G-protein membrane receptors, including rod and cone photoreceptors and adrenergic receptors.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
The study of the generation and behavior of electrical charges in living organisms particularly the nervous system and the effects of electricity on living organisms.
The largest family of cell surface receptors involved in SIGNAL TRANSDUCTION. They share a common structure and signal through HETEROTRIMERIC G-PROTEINS.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
The rate dynamics in chemical or physical systems.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Quantitative determination of receptor (binding) proteins in body fluids or tissue using radioactively labeled binding reagents (e.g., antibodies, intracellular receptors, plasma binders).
A family of voltage-gated potassium channels that are characterized by long N-terminal and C-terminal intracellular tails. They are named from the Drosophila protein whose mutation causes abnormal leg shaking under ether anesthesia. Their activation kinetics are dependent on extracellular MAGNESIUM and PROTON concentration.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue.
A subgroup of TRP cation channels named after vanilloid receptor. They are very sensitive to TEMPERATURE and hot spicy food and CAPSAICIN. They have the TRP domain and ANKYRIN repeats. Selectivity for CALCIUM over SODIUM ranges from 3 to 100 fold.
A purinergic P2X neurotransmitter receptor that plays a role in pain sensation signaling and regulation of inflammatory processes.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Potassium channels where the flow of K+ ions into the cell is greater than the outward flow.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
A family of proteins involved in the transport of organic cations. They play an important role in the elimination of a variety of endogenous substances, xenobiotics, and their metabolites from the body.
A class of G-protein-coupled receptors that react to varying extracellular CALCIUM levels. Calcium-sensing receptors in the PARATHYROID GLANDS play an important role in the maintenance of calcium HOMEOSTASIS by regulating the release of PARATHYROID HORMONE. They differ from INTRACELLULAR CALCIUM-SENSING PROTEINS which sense intracellular calcium levels.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Cell membrane glycoproteins that are selectively permeable to potassium ions. At least eight major groups of K channels exist and they are made up of dozens of different subunits.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
Ion channels that specifically allow the passage of SODIUM ions. A variety of specific sodium channel subtypes are involved in serving specialized functions such as neuronal signaling, CARDIAC MUSCLE contraction, and KIDNEY function.
A type of FLUORESCENCE SPECTROSCOPY using two FLUORESCENT DYES with overlapping emission and absorption spectra, which is used to indicate proximity of labeled molecules. This technique is useful for studying interactions of molecules and PROTEIN FOLDING.
An eph family receptor found in a number of tissues including BRAIN; LUNG; KIDNEY; PANCREAS; INTESTINE; and HEART. During embryogenesis EphB3 receptor is expressed at high levels in the brain.
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
A subclass of serotonin receptors that form cation channels and mediate signal transduction by depolarizing the cell membrane. The cation channels are formed from 5 receptor subunits. When stimulated the receptors allow the selective passage of SODIUM; POTASSIUM; and CALCIUM.
A subgroup of TRP cation channels named after melastatin protein. They have the TRP domain but lack ANKYRIN repeats. Enzyme domains in the C-terminus leads to them being called chanzymes.
A voltage-gated sodium channel subtype that mediates the sodium ion PERMEABILITY of CARDIOMYOCYTES. Defects in the SCN5A gene, which codes for the alpha subunit of this sodium channel, are associated with a variety of CARDIAC DISEASES that result from loss of sodium channel function.
Incorporation of biotinyl groups into molecules.
Potassium channel whose permeability to ions is extremely sensitive to the transmembrane potential difference. The opening of these channels is induced by the membrane depolarization of the ACTION POTENTIAL.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
A family of heterotrimeric GTP-binding protein alpha subunits that activate TYPE C PHOSPHOLIPASES dependent signaling pathways. The Gq-G11 part of the name is also spelled Gq/G11.
A secreted protein that associates with TOLL-LIKE RECEPTOR 4 and is essential for receptor recognition of LIPOPOLYSACCHARIDES.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
Signal transduction mechanisms whereby calcium mobilization (from outside the cell or from intracellular storage pools) to the cytoplasm is triggered by external stimuli. Calcium signals are often seen to propagate as waves, oscillations, spikes, sparks, or puffs. The calcium acts as an intracellular messenger by activating calcium-responsive proteins.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)
A delayed rectifier subtype of shaker potassium channels that conducts a delayed rectifier current. It contributes to ACTION POTENTIAL repolarization of MYOCYTES in HEART ATRIA.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.
A pattern recognition receptor that forms heterodimers with other TOLL-LIKE RECEPTORS. It interacts with multiple ligands including PEPTIDOGLYCAN, bacterial LIPOPROTEINS, lipoarabinomannan, and a variety of PORINS.
Transport proteins that carry specific substances in the blood or across cell membranes.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.

Mammalian Notum induces the release of glypicans and other GPI-anchored proteins from the cell surface. (1/10093)

Glypicans are heparan sulfate proteoglycans that are attached to the cell surface by a GPI (glycosylphosphatidylinositol)anchor. Glypicans regulate the activity of Wnts, Hedgehogs,bone morphogenetic proteins and fibroblast growth factors. In the particular case of Wnts, it has been proposed that GPI-anchored glypicans stimulate Wnt signalling by facilitating and/or stabilizing the interaction between Wnts and their cell surface receptors. On the other hand, when glypicans are secreted to the extracellular environment, they can act as competitive inhibitors of Wnt. Genetic screens in Drosophila have recently identified a novel inhibitor of Wnt signalling named Notum. The Wnt inhibiting activity of Notum was associated with its ability to release Dlp [Dally (Division abnormally delayed)-like protein; a Drosophila glypican] from the cell surface by cleaving the GPI anchor. Because these studies showed that the other Drosophila glypican Dally was not released from the cell surface by Notum,it remains unclear whether this enzyme is able to cleave glypicans from mammalian cells. Furthermore, it is also not known whether Notum cleaves GPI-anchored proteins that are not members of the glypican family. Here, we show that mammalian Notum can cleave several mammalian glypicans. Moreover, we demonstrate that Notum is able to release GPI-anchored proteins other than glypicans. Another important finding of the present study is that,unlike GPI-phospholipase D, the other mammalian enzyme that cleaves GPI-anchored proteins, Notum is active in the extracellular environment. Finally, by using a cellular system in which GPC3 (glypican-3) stimulates Wnt signalling, we show that Notum can act as a negative regulator of this growth factor.  (+info)

alpha-Actinin interacts with rapsyn in agrin-stimulated AChR clustering. (2/10093)

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Influence of brain-derived neurotrophic factor on pathfinding of dentate granule cell axons, the hippocampal mossy fibers. (3/10093)

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Effective gene-viral therapy of leukemia by a new fiber chimeric oncolytic adenovirus expressing TRAIL: in vitro and in vivo evaluation. (4/10093)

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A novel human monoclonal antibody that binds with high affinity to mesothelin-expressing cells and kills them by antibody-dependent cell-mediated cytotoxicity. (5/10093)

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Regulation of dopamine transporter activity by carboxypeptidase E. (6/10093)

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Soluble c-Met receptors inhibit phosphorylation of c-Met and growth of hepatocyte growth factor: c-Met-dependent tumors in animal models. (7/10093)

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Selenoprotein P regulation by the glucocorticoid receptor. (8/10093)

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HEK293 cells, also known as human embryonic kidney 293 cells, are a line of cells used in scientific research. They were originally derived from human embryonic kidney cells and have been adapted to grow in a lab setting. HEK293 cells are widely used in molecular biology and biochemistry because they can be easily transfected (a process by which DNA is introduced into cells) and highly express foreign genes. As a result, they are often used to produce proteins for structural and functional studies. It's important to note that while HEK293 cells are derived from human tissue, they have been grown in the lab for many generations and do not retain the characteristics of the original embryonic kidney cells.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

EphA3 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a transmembrane protein involved in cell-cell communication and signal transduction. The EphA3 receptor specifically binds to ephrin-A5, its ligand, leading to various intracellular signaling events that regulate cell behavior, including cell migration, adhesion, and differentiation.

EphA3 is widely expressed in various tissues, including the nervous system, hematopoietic cells, and epithelial cells. In the nervous system, EphA3 plays a crucial role in axon guidance and neuronal positioning during development. In hematopoietic cells, it has been implicated in the regulation of immune cell function and the development of certain types of leukemia.

Mutations or aberrant expression of EphA3 have been associated with several diseases, including cancer, making it a potential target for therapeutic intervention.

Patch-clamp techniques are a group of electrophysiological methods used to study ion channels and other electrical properties of cells. These techniques were developed by Erwin Neher and Bert Sakmann, who were awarded the Nobel Prize in Physiology or Medicine in 1991 for their work. The basic principle of patch-clamp techniques involves creating a high resistance seal between a glass micropipette and the cell membrane, allowing for the measurement of current flowing through individual ion channels or groups of channels.

There are several different configurations of patch-clamp techniques, including:

1. Cell-attached configuration: In this configuration, the micropipette is attached to the outer surface of the cell membrane, and the current flowing across a single ion channel can be measured. This configuration allows for the study of the properties of individual channels in their native environment.
2. Whole-cell configuration: Here, the micropipette breaks through the cell membrane, creating a low resistance electrical connection between the pipette and the inside of the cell. This configuration allows for the measurement of the total current flowing across all ion channels in the cell membrane.
3. Inside-out configuration: In this configuration, the micropipette is pulled away from the cell after establishing a seal, resulting in the exposure of the inner surface of the cell membrane to the solution in the pipette. This configuration allows for the study of the properties of ion channels in isolation from other cellular components.
4. Outside-out configuration: Here, the micropipette is pulled away from the cell after establishing a seal, resulting in the exposure of the outer surface of the cell membrane to the solution in the pipette. This configuration allows for the study of the properties of ion channels in their native environment, but with the ability to control the composition of the extracellular solution.

Patch-clamp techniques have been instrumental in advancing our understanding of ion channel function and have contributed to numerous breakthroughs in neuroscience, pharmacology, and physiology.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Calcium is an essential mineral that is vital for various physiological processes in the human body. The medical definition of calcium is as follows:

Calcium (Ca2+) is a crucial cation and the most abundant mineral in the human body, with approximately 99% of it found in bones and teeth. It plays a vital role in maintaining structural integrity, nerve impulse transmission, muscle contraction, hormonal secretion, blood coagulation, and enzyme activation.

Calcium homeostasis is tightly regulated through the interplay of several hormones, including parathyroid hormone (PTH), calcitonin, and vitamin D. Dietary calcium intake, absorption, and excretion are also critical factors in maintaining optimal calcium levels in the body.

Hypocalcemia refers to low serum calcium levels, while hypercalcemia indicates high serum calcium levels. Both conditions can have detrimental effects on various organ systems and require medical intervention to correct.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Ion channel gating refers to the process by which ion channels in cell membranes open and close in response to various stimuli, allowing ions such as sodium, potassium, and calcium to flow into or out of the cell. This movement of ions is crucial for many physiological processes, including the generation and transmission of electrical signals in nerve cells, muscle contraction, and the regulation of hormone secretion.

Ion channel gating can be regulated by various factors, including voltage changes across the membrane (voltage-gated channels), ligand binding (ligand-gated channels), mechanical stress (mechanosensitive channels), or other intracellular signals (second messenger-gated channels). The opening and closing of ion channels are highly regulated and coordinated processes that play a critical role in maintaining the proper functioning of cells and organ systems.

Transient Receptor Potential Canonical (TRPC) cation channels are a subfamily of the TRP superfamily of non-selective cation channels. They are widely expressed in various tissues and play crucial roles in many cellular processes, including sensory perception, cell proliferation, and migration. TRPC channels are permeable to both monovalent (sodium and potassium) and divalent (calcium and magnesium) cations, and their activation can lead to a rise in intracellular calcium concentration, which in turn regulates various downstream signaling pathways. TRPC channels can be activated by a variety of stimuli, including G protein-coupled receptors, receptor tyrosine kinases, and mechanical stress. Mutations in TRPC genes have been associated with several human diseases, including hereditary hearing loss, cardiovascular disorders, and neurological conditions.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Complementary DNA (cDNA) is a type of DNA that is synthesized from a single-stranded RNA molecule through the process of reverse transcription. In this process, the enzyme reverse transcriptase uses an RNA molecule as a template to synthesize a complementary DNA strand. The resulting cDNA is therefore complementary to the original RNA molecule and is a copy of its coding sequence, but it does not contain non-coding regions such as introns that are present in genomic DNA.

Complementary DNA is often used in molecular biology research to study gene expression, protein function, and other genetic phenomena. For example, cDNA can be used to create cDNA libraries, which are collections of cloned cDNA fragments that represent the expressed genes in a particular cell type or tissue. These libraries can then be screened for specific genes or gene products of interest. Additionally, cDNA can be used to produce recombinant proteins in heterologous expression systems, allowing researchers to study the structure and function of proteins that may be difficult to express or purify from their native sources.

Membrane potential is the electrical potential difference across a cell membrane, typically for excitable cells such as nerve and muscle cells. It is the difference in electric charge between the inside and outside of a cell, created by the selective permeability of the cell membrane to different ions. The resting membrane potential of a typical animal cell is around -70 mV, with the interior being negative relative to the exterior. This potential is generated and maintained by the active transport of ions across the membrane, primarily through the action of the sodium-potassium pump. Membrane potentials play a crucial role in many physiological processes, including the transmission of nerve impulses and the contraction of muscle cells.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Immunoprecipitation (IP) is a research technique used in molecular biology and immunology to isolate specific antigens or antibodies from a mixture. It involves the use of an antibody that recognizes and binds to a specific antigen, which is then precipitated out of solution using various methods, such as centrifugation or chemical cross-linking.

In this technique, an antibody is first incubated with a sample containing the antigen of interest. The antibody specifically binds to the antigen, forming an immune complex. This complex can then be captured by adding protein A or G agarose beads, which bind to the constant region of the antibody. The beads are then washed to remove any unbound proteins, leaving behind the precipitated antigen-antibody complex.

Immunoprecipitation is a powerful tool for studying protein-protein interactions, post-translational modifications, and signal transduction pathways. It can also be used to detect and quantify specific proteins in biological samples, such as cells or tissues, and to identify potential biomarkers of disease.

Arrestins are a family of proteins that play a crucial role in regulating G protein-coupled receptor (GPCR) signaling. There are four main types of arrestins: visual arrestin (also known as arr1 or S-arrestin), β-arrestin1 (also known as arr2 or Kon/Vec), β-arrestin2 (also known as arr3 or hTHT), and arrestin-domain containing protein 1 (ARRDC1).

Arrestins bind to the intracellular domains of activated GPCRs, which leads to several outcomes:

1. They prevent further activation of G proteins by the receptor, effectively "arresting" the signal transduction process.
2. They promote the internalization (endocytosis) of the receptor from the cell membrane into endosomes, where it can be either degraded or recycled back to the cell surface.
3. They act as scaffolds for various signaling complexes and mediate interactions between GPCRs and other intracellular signaling proteins, leading to the activation of different signaling pathways.

Overall, arrestins play a critical role in fine-tuning GPCR signaling, ensuring appropriate cellular responses to hormones, neurotransmitters, and other extracellular signals.

A dose-response relationship in the context of drugs refers to the changes in the effects or symptoms that occur as the dose of a drug is increased or decreased. Generally, as the dose of a drug is increased, the severity or intensity of its effects also increases. Conversely, as the dose is decreased, the effects of the drug become less severe or may disappear altogether.

The dose-response relationship is an important concept in pharmacology and toxicology because it helps to establish the safe and effective dosage range for a drug. By understanding how changes in the dose of a drug affect its therapeutic and adverse effects, healthcare providers can optimize treatment plans for their patients while minimizing the risk of harm.

The dose-response relationship is typically depicted as a curve that shows the relationship between the dose of a drug and its effect. The shape of the curve may vary depending on the drug and the specific effect being measured. Some drugs may have a steep dose-response curve, meaning that small changes in the dose can result in large differences in the effect. Other drugs may have a more gradual dose-response curve, where larger changes in the dose are needed to produce significant effects.

In addition to helping establish safe and effective dosages, the dose-response relationship is also used to evaluate the potential therapeutic benefits and risks of new drugs during clinical trials. By systematically testing different doses of a drug in controlled studies, researchers can identify the optimal dosage range for the drug and assess its safety and efficacy.

Confocal microscopy is a powerful imaging technique used in medical and biological research to obtain high-resolution, contrast-rich images of thick samples. This super-resolution technology provides detailed visualization of cellular structures and processes at various depths within a specimen.

In confocal microscopy, a laser beam focused through a pinhole illuminates a small spot within the sample. The emitted fluorescence or reflected light from this spot is then collected by a detector, passing through a second pinhole that ensures only light from the focal plane reaches the detector. This process eliminates out-of-focus light, resulting in sharp images with improved contrast compared to conventional widefield microscopy.

By scanning the laser beam across the sample in a raster pattern and collecting fluorescence at each point, confocal microscopy generates optical sections of the specimen. These sections can be combined to create three-dimensional reconstructions, allowing researchers to study cellular architecture and interactions within complex tissues.

Confocal microscopy has numerous applications in medical research, including studying protein localization, tracking intracellular dynamics, analyzing cell morphology, and investigating disease mechanisms at the cellular level. Additionally, it is widely used in clinical settings for diagnostic purposes, such as analyzing skin lesions or detecting pathogens in patient samples.

Green Fluorescent Protein (GFP) is not a medical term per se, but a scientific term used in the field of molecular biology. GFP is a protein that exhibits bright green fluorescence when exposed to light, particularly blue or ultraviolet light. It was originally discovered in the jellyfish Aequorea victoria.

In medical and biological research, scientists often use recombinant DNA technology to introduce the gene for GFP into other organisms, including bacteria, plants, and animals, including humans. This allows them to track the expression and localization of specific genes or proteins of interest in living cells, tissues, or even whole organisms.

The ability to visualize specific cellular structures or processes in real-time has proven invaluable for a wide range of research areas, from studying the development and function of organs and organ systems to understanding the mechanisms of diseases and the effects of therapeutic interventions.

Electrophysiology is a branch of medicine that deals with the electrical activities of the body, particularly the heart. In a medical context, electrophysiology studies (EPS) are performed to assess abnormal heart rhythms (arrhythmias) and to evaluate the effectiveness of certain treatments, such as medication or pacemakers.

During an EPS, electrode catheters are inserted into the heart through blood vessels in the groin or neck. These catheters can record the electrical activity of the heart and stimulate it to help identify the source of the arrhythmia. The information gathered during the study can help doctors determine the best course of treatment for each patient.

In addition to cardiac electrophysiology, there are also other subspecialties within electrophysiology, such as neuromuscular electrophysiology, which deals with the electrical activity of the nervous system and muscles.

G-protein-coupled receptors (GPCRs) are a family of membrane receptors that play an essential role in cellular signaling and communication. These receptors possess seven transmembrane domains, forming a structure that spans the lipid bilayer of the cell membrane. They are called "G-protein-coupled" because they interact with heterotrimeric G proteins upon activation, which in turn modulate various downstream signaling pathways.

When an extracellular ligand binds to a GPCR, it causes a conformational change in the receptor's structure, leading to the exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on the associated G protein's α subunit. This exchange triggers the dissociation of the G protein into its α and βγ subunits, which then interact with various effector proteins to elicit cellular responses.

There are four main families of GPCRs, classified based on their sequence similarities and downstream signaling pathways:

1. Gq-coupled receptors: These receptors activate phospholipase C (PLC), which leads to the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). IP3 induces calcium release from intracellular stores, while DAG activates protein kinase C (PKC).
2. Gs-coupled receptors: These receptors activate adenylyl cyclase, which increases the production of cyclic adenosine monophosphate (cAMP) and subsequently activates protein kinase A (PKA).
3. Gi/o-coupled receptors: These receptors inhibit adenylyl cyclase, reducing cAMP levels and modulating PKA activity. Additionally, they can activate ion channels or regulate other signaling pathways through the βγ subunits.
4. G12/13-coupled receptors: These receptors primarily activate RhoGEFs, which in turn activate RhoA and modulate cytoskeletal organization and cellular motility.

GPCRs are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and sensory perception. Dysregulation of GPCR function has been implicated in numerous diseases, making them attractive targets for drug development.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Protein isoforms are different forms or variants of a protein that are produced from a single gene through the process of alternative splicing, where different exons (or parts of exons) are included in the mature mRNA molecule. This results in the production of multiple, slightly different proteins that share a common core structure but have distinct sequences and functions. Protein isoforms can also arise from genetic variations such as single nucleotide polymorphisms or mutations that alter the protein-coding sequence of a gene. These differences in protein sequence can affect the stability, localization, activity, or interaction partners of the protein isoform, leading to functional diversity and specialization within cells and organisms.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

A radioligand assay is a type of in vitro binding assay used in molecular biology and pharmacology to measure the affinity and quantity of a ligand (such as a drug or hormone) to its specific receptor. In this technique, a small amount of a radioactively labeled ligand, also known as a radioligand, is introduced to a sample containing the receptor of interest. The radioligand binds competitively with other unlabeled ligands present in the sample for the same binding site on the receptor. After allowing sufficient time for binding, the reaction is stopped, and the amount of bound radioligand is measured using a technique such as scintillation counting. The data obtained from this assay can be used to determine the dissociation constant (Kd) and maximum binding capacity (Bmax) of the receptor-ligand interaction, which are important parameters in understanding the pharmacological properties of drugs and other ligands.

Ether-à-go-go (EAG) potassium channels are a type of voltage-gated potassium channel that are widely expressed in the heart, brain, and other tissues. They are named after the ethereal dance movements observed in fruit flies with mutations in these channels.

EAG potassium channels play important roles in regulating electrical excitability and signaling in excitable cells. In the heart, they help to control the duration of the action potential and the refractory period, which is critical for maintaining normal heart rhythm. In the brain, they are involved in regulating neuronal excitability and neurotransmitter release.

Mutations in EAG potassium channels have been associated with various human diseases, including cardiac arrhythmias, epilepsy, and bipolar disorder. The medical definition of "Ether-A-Go-Go Potassium Channels" refers to the genetic components that make up these channels and their role in physiological processes and disease states.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Cyclic adenosine monophosphate (cAMP) is a key secondary messenger in many biological processes, including the regulation of metabolism, gene expression, and cellular excitability. It is synthesized from adenosine triphosphate (ATP) by the enzyme adenylyl cyclase and is degraded by the enzyme phosphodiesterase.

In the body, cAMP plays a crucial role in mediating the effects of hormones and neurotransmitters on target cells. For example, when a hormone binds to its receptor on the surface of a cell, it can activate a G protein, which in turn activates adenylyl cyclase to produce cAMP. The increased levels of cAMP then activate various effector proteins, such as protein kinases, which go on to regulate various cellular processes.

Overall, the regulation of cAMP levels is critical for maintaining proper cellular function and homeostasis, and abnormalities in cAMP signaling have been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Enzyme activation refers to the process by which an enzyme becomes biologically active and capable of carrying out its specific chemical or biological reaction. This is often achieved through various post-translational modifications, such as proteolytic cleavage, phosphorylation, or addition of cofactors or prosthetic groups to the enzyme molecule. These modifications can change the conformation or structure of the enzyme, exposing or creating a binding site for the substrate and allowing the enzymatic reaction to occur.

For example, in the case of proteolytic cleavage, an inactive precursor enzyme, known as a zymogen, is cleaved into its active form by a specific protease. This is seen in enzymes such as trypsin and chymotrypsin, which are initially produced in the pancreas as inactive precursors called trypsinogen and chymotrypsinogen, respectively. Once they reach the small intestine, they are activated by enteropeptidase, a protease that cleaves a specific peptide bond, releasing the active enzyme.

Phosphorylation is another common mechanism of enzyme activation, where a phosphate group is added to a specific serine, threonine, or tyrosine residue on the enzyme by a protein kinase. This modification can alter the conformation of the enzyme and create a binding site for the substrate, allowing the enzymatic reaction to occur.

Enzyme activation is a crucial process in many biological pathways, as it allows for precise control over when and where specific reactions take place. It also provides a mechanism for regulating enzyme activity in response to various signals and stimuli, such as hormones, neurotransmitters, or changes in the intracellular environment.

Calcium channels are specialized proteins that span the membrane of cells and allow calcium ions (Ca²+) to flow in and out of the cell. They are crucial for many physiological processes, including muscle contraction, neurotransmitter release, hormone secretion, and gene expression.

There are several types of calcium channels, classified based on their biophysical and pharmacological properties. The most well-known are:

1. Voltage-gated calcium channels (VGCCs): These channels are activated by changes in the membrane potential. They are further divided into several subtypes, including L-type, P/Q-type, N-type, R-type, and T-type. VGCCs play a critical role in excitation-contraction coupling in muscle cells and neurotransmitter release in neurons.
2. Receptor-operated calcium channels (ROCCs): These channels are activated by the binding of an extracellular ligand, such as a hormone or neurotransmitter, to a specific receptor on the cell surface. ROCCs are involved in various physiological processes, including smooth muscle contraction and platelet activation.
3. Store-operated calcium channels (SOCCs): These channels are activated by the depletion of intracellular calcium stores, such as those found in the endoplasmic reticulum. SOCCs play a critical role in maintaining calcium homeostasis and signaling within cells.

Dysregulation of calcium channel function has been implicated in various diseases, including hypertension, arrhythmias, migraine, epilepsy, and neurodegenerative disorders. Therefore, calcium channels are an important target for drug development and therapy.

Transient receptor potential vanilloid (TRPV) cation channels are a subfamily of transient receptor potential (TRP) channels, which are non-selective cation channels that play important roles in various physiological processes such as nociception, thermosensation, and mechanosensation. TRPV channels are activated by a variety of stimuli including temperature, chemical ligands, and mechanical forces.

TRPV channels are composed of six transmembrane domains with intracellular N- and C-termini. The TRPV subfamily includes six members: TRPV1 to TRPV6. Among them, TRPV1 is also known as the vanilloid receptor 1 (VR1) and is activated by capsaicin, the active component of hot chili peppers, as well as noxious heat. TRPV2 is activated by noxious heat and mechanical stimuli, while TRPV3 and TRPV4 are activated by warm temperatures and various chemical ligands. TRPV5 and TRPV6 are primarily involved in calcium transport and are activated by low pH and divalent cations.

TRPV channels play important roles in pain sensation, neurogenic inflammation, and temperature perception. Dysfunction of these channels has been implicated in various pathological conditions such as chronic pain, inflammatory diseases, and cancer. Therefore, TRPV channels are considered promising targets for the development of novel therapeutics for these conditions.

Purinergic P2X7 receptors are a type of ligand-gated ion channel that are activated by the binding of extracellular adenosine triphosphate (ATP) to the P2X7 receptor subunit. These receptors play important roles in various physiological and pathophysiological processes, including inflammation, immune response, pain perception, and cell death.

Upon activation of P2X7 receptors, there is an increase in membrane permeability to small cations such as Na+, K+, and Ca2+, which can lead to the depolarization of the cell membrane. Prolonged activation of these receptors can result in the formation of large pores that allow for the passage of larger molecules, including inflammatory mediators and even small proteins. This can ultimately lead to the induction of apoptosis or necrosis in certain cells.

P2X7 receptors are widely expressed in various tissues, including the brain, spinal cord, immune cells, and epithelial cells. In recent years, there has been growing interest in targeting P2X7 receptors for therapeutic purposes, particularly in the context of inflammatory diseases and chronic pain.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Small interfering RNA (siRNA) is a type of short, double-stranded RNA molecule that plays a role in the RNA interference (RNAi) pathway. The RNAi pathway is a natural cellular process that regulates gene expression by targeting and destroying specific messenger RNA (mRNA) molecules, thereby preventing the translation of those mRNAs into proteins.

SiRNAs are typically 20-25 base pairs in length and are generated from longer double-stranded RNA precursors called hairpin RNAs or dsRNAs by an enzyme called Dicer. Once generated, siRNAs associate with a protein complex called the RNA-induced silencing complex (RISC), which uses one strand of the siRNA (the guide strand) to recognize and bind to complementary sequences in the target mRNA. The RISC then cleaves the target mRNA, leading to its degradation and the inhibition of protein synthesis.

SiRNAs have emerged as a powerful tool for studying gene function and have shown promise as therapeutic agents for a variety of diseases, including viral infections, cancer, and genetic disorders. However, their use as therapeutics is still in the early stages of development, and there are challenges associated with delivering siRNAs to specific cells and tissues in the body.

Inwardly rectifying potassium channels (Kir) are a type of potassium channel that allow for the selective passage of potassium ions (K+) across cell membranes. The term "inwardly rectifying" refers to their unique property of allowing potassium ions to flow more easily into the cell (inward current) than out of the cell (outward current). This characteristic is due to the voltage-dependent blockage of these channels by intracellular magnesium and polyamines at depolarized potentials.

These channels play crucial roles in various physiological processes, including:

1. Resting membrane potential maintenance: Kir channels help establish and maintain the negative resting membrane potential in cells by facilitating potassium efflux when the membrane potential is near the potassium equilibrium potential (Ek).
2. Action potential repolarization: In excitable cells like neurons and muscle fibers, Kir channels contribute to the rapid repolarization phase of action potentials, allowing for proper electrical signaling.
3. Cell volume regulation: Kir channels are involved in regulating cell volume by mediating potassium influx during osmotic stress or changes in intracellular ion concentrations.
4. Insulin secretion: In pancreatic β-cells, Kir channels control the membrane potential and calcium signaling necessary for insulin release.
5. Renal function: Kir channels are essential for maintaining electrolyte balance and controlling renal tubular transport in the kidneys.

There are several subfamilies of inwardly rectifying potassium channels (Kir1-7), each with distinct biophysical properties, tissue distributions, and functions. Mutations in genes encoding these channels can lead to various human diseases, including cardiac arrhythmias, epilepsy, and Bartter syndrome.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Luminescent proteins are a type of protein that emit light through a chemical reaction, rather than by absorbing and re-emitting light like fluorescent proteins. This process is called bioluminescence. The light emitted by luminescent proteins is often used in scientific research as a way to visualize and track biological processes within cells and organisms.

One of the most well-known luminescent proteins is Green Fluorescent Protein (GFP), which was originally isolated from jellyfish. However, GFP is actually a fluorescent protein, not a luminescent one. A true example of a luminescent protein is the enzyme luciferase, which is found in fireflies and other bioluminescent organisms. When luciferase reacts with its substrate, luciferin, it produces light through a process called oxidation.

Luminescent proteins have many applications in research, including as reporters for gene expression, as markers for protein-protein interactions, and as tools for studying the dynamics of cellular processes. They are also used in medical imaging and diagnostics, as well as in the development of new therapies.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

A ligand, in the context of biochemistry and medicine, is a molecule that binds to a specific site on a protein or a larger biomolecule, such as an enzyme or a receptor. This binding interaction can modify the function or activity of the target protein, either activating it or inhibiting it. Ligands can be small molecules, like hormones or neurotransmitters, or larger structures, like antibodies. The study of ligand-protein interactions is crucial for understanding cellular processes and developing drugs, as many therapeutic compounds function by binding to specific targets within the body.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Organic cation transport proteins (OCTs) are a group of membrane transporters that facilitate the movement of organic cations across biological membranes. These transporters play an essential role in the absorption, distribution, and elimination of various endogenous and exogenous substances, including drugs and toxins.

There are four main types of OCTs, namely OCT1, OCT2, OCT3, and OCTN1 (also known as novel organic cation transporter 1 or OCT6). These proteins belong to the solute carrier (SLC) family, specifically SLC22A.

OCTs have a broad substrate specificity and can transport various organic cations, such as neurotransmitters (e.g., serotonin, dopamine, histamine), endogenous compounds (e.g., creatinine, choline), and drugs (e.g., metformin, quinidine, morphine). The transport process is typically sodium-independent and can occur in both directions, depending on the concentration gradient of the substrate.

OCTs are widely expressed in various tissues, including the liver, kidney, intestine, brain, heart, and placenta. Their expression patterns and functions vary among different OCT types, contributing to their diverse roles in physiology and pharmacology. Dysfunction of OCTs has been implicated in several diseases, such as drug toxicity, neurodegenerative disorders, and cancer.

In summary, organic cation transport proteins are membrane transporters that facilitate the movement of organic cations across biological membranes, playing crucial roles in the absorption, distribution, and elimination of various substances, including drugs and toxins.

Calcium-sensing receptors (CaSR) are a type of G protein-coupled receptor that play a crucial role in the regulation of extracellular calcium homeostasis. They are widely expressed in various tissues, including the parathyroid gland, kidney, and bone.

The primary function of CaSR is to detect changes in extracellular calcium concentrations and transmit signals to regulate the release of parathyroid hormone (PTH) from the parathyroid gland. When the concentration of extracellular calcium increases, CaSR is activated, which leads to a decrease in PTH secretion, thereby preventing further elevation of calcium levels. Conversely, when calcium levels decrease, CaSR is inhibited, leading to an increase in PTH release and restoration of normal calcium levels.

In addition to regulating calcium homeostasis, CaSR also plays a role in other physiological processes, including cell proliferation, differentiation, and apoptosis. Dysregulation of CaSR has been implicated in various diseases, such as hyperparathyroidism, hypoparathyroidism, and cancer. Therefore, understanding the function and regulation of CaSR is essential for developing new therapeutic strategies to treat these conditions.

A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.

The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.

The main components of a two-hybrid system include:

1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)

The two-hybrid system technique has several advantages, including:

1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis

However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.

Potassium channels are membrane proteins that play a crucial role in regulating the electrical excitability of cells, including cardiac, neuronal, and muscle cells. These channels facilitate the selective passage of potassium ions (K+) across the cell membrane, maintaining the resting membrane potential and shaping action potentials. They are composed of four or six subunits that assemble to form a central pore through which potassium ions move down their electrochemical gradient. Potassium channels can be modulated by various factors such as voltage, ligands, mechanical stimuli, or temperature, allowing cells to fine-tune their electrical properties and respond to different physiological demands. Dysfunction of potassium channels has been implicated in several diseases, including cardiac arrhythmias, epilepsy, and neurodegenerative disorders.

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

Sodium channels are specialized protein structures that are embedded in the membranes of excitable cells, such as nerve and muscle cells. They play a crucial role in the generation and transmission of electrical signals in these cells. Sodium channels are responsible for the rapid influx of sodium ions into the cell during the initial phase of an action potential, which is the electrical signal that travels along the membrane of a neuron or muscle fiber. This sudden influx of sodium ions causes the membrane potential to rapidly reverse, leading to the depolarization of the cell. After the action potential, the sodium channels close and become inactivated, preventing further entry of sodium ions and helping to restore the resting membrane potential.

Sodium channels are composed of a large alpha subunit and one or two smaller beta subunits. The alpha subunit forms the ion-conducting pore, while the beta subunits play a role in modulating the function and stability of the channel. Mutations in sodium channel genes have been associated with various inherited diseases, including certain forms of epilepsy, cardiac arrhythmias, and muscle disorders.

Fluorescence Resonance Energy Transfer (FRET) is not strictly a medical term, but it is a fundamental concept in biophysical and molecular biology research, which can have medical applications. Here's the definition of FRET:

Fluorescence Resonance Energy Transfer (FRET) is a distance-dependent energy transfer process between two fluorophores, often referred to as a donor and an acceptor. The process occurs when the emission spectrum of the donor fluorophore overlaps with the excitation spectrum of the acceptor fluorophore. When the donor fluorophore is excited, it can transfer its energy to the acceptor fluorophore through non-radiative dipole-dipole coupling, resulting in the emission of light from the acceptor at a longer wavelength than that of the donor.

FRET efficiency depends on several factors, including the distance between the two fluorophores, their relative orientation, and the spectral overlap between their excitation and emission spectra. FRET is typically efficient when the distance between the donor and acceptor is less than 10 nm (nanometers), making it a powerful tool for measuring molecular interactions, conformational changes, and distances at the molecular level.

In medical research, FRET has been used to study various biological processes, such as protein-protein interactions, enzyme kinetics, and gene regulation. It can also be used in developing biosensors for detecting specific molecules or analytes in clinical samples, such as blood or tissue.

EphB3 is a type of receptor tyrosine kinase that belongs to the Eph family of receptors. It is a transmembrane protein that plays a crucial role in cell signaling and communication, particularly during embryonic development and tissue organization. The EphB3 receptor binds to ephrin-B ligands, which are also transmembrane proteins expressed on neighboring cells.

The binding of ephrin-B to EphB3 initiates a bidirectional signaling process that regulates various cellular processes such as cell adhesion, migration, and repulsion. This interaction is important for the formation of boundaries between different tissues, axon guidance, and synaptic plasticity in the nervous system.

Mutations in the EphB3 gene have been associated with several human diseases, including cancer, immune disorders, and neurological conditions. Therefore, understanding the function and regulation of EphB3 receptors is essential for developing novel therapeutic strategies to treat these diseases.

Glycosylation is the enzymatic process of adding a sugar group, or glycan, to a protein, lipid, or other organic molecule. This post-translational modification plays a crucial role in modulating various biological functions, such as protein stability, trafficking, and ligand binding. The structure and composition of the attached glycans can significantly influence the functional properties of the modified molecule, contributing to cell-cell recognition, signal transduction, and immune response regulation. Abnormal glycosylation patterns have been implicated in several disease states, including cancer, diabetes, and neurodegenerative disorders.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

COS cells are a type of cell line that are commonly used in molecular biology and genetic research. The name "COS" is an acronym for "CV-1 in Origin," as these cells were originally derived from the African green monkey kidney cell line CV-1. COS cells have been modified through genetic engineering to express high levels of a protein called SV40 large T antigen, which allows them to efficiently take up and replicate exogenous DNA.

There are several different types of COS cells that are commonly used in research, including COS-1, COS-3, and COS-7 cells. These cells are widely used for the production of recombinant proteins, as well as for studies of gene expression, protein localization, and signal transduction.

It is important to note that while COS cells have been a valuable tool in scientific research, they are not without their limitations. For example, because they are derived from monkey kidney cells, there may be differences in the way that human genes are expressed or regulated in these cells compared to human cells. Additionally, because COS cells express SV40 large T antigen, they may have altered cell cycle regulation and other phenotypic changes that could affect experimental results. Therefore, it is important to carefully consider the choice of cell line when designing experiments and interpreting results.

'Receptors, Serotonin, 5-HT3' refer to a specific type of serotonin receptor called the 5-HT3 receptor, which is a ligand-gated ion channel found in the cell membrane. Serotonin, also known as 5-hydroxytryptamine (5-HT), is a neurotransmitter that plays a role in various physiological functions, including mood regulation, appetite control, and nausea.

The 5-HT3 receptor is activated by serotonin and mediates fast excitatory synaptic transmission in the central and peripheral nervous systems. It is permeable to sodium (Na+), potassium (K+), and calcium (Ca2+) ions, allowing for the rapid depolarization of neurons and the initiation of action potentials.

The 5-HT3 receptor has been a target for drug development, particularly in the treatment of chemotherapy-induced nausea and vomiting, as well as irritable bowel syndrome. Antagonists of the 5-HT3 receptor, such as ondansetron and granisetron, work by blocking the receptor and preventing serotonin from activating it, thereby reducing symptoms of nausea and vomiting.

Transient Receptor Potential Melastatin (TRPM) cation channels are a subfamily of the transient receptor potential (TRP) channel superfamily, which are non-selective cation channels that play important roles in various cellular processes such as sensory perception, cell proliferation, and migration.

The TRPM subfamily consists of eight members (TRPM1-8), each with distinct functional properties and expression patterns. These channels are permeable to both monovalent and divalent cations, including calcium (Ca^2+^) and magnesium (Mg^2+^).

TRPM channels can be activated by a variety of stimuli, such as changes in temperature, voltage, osmolarity, and chemical ligands. For example, TRPM8 is known to be activated by cold temperatures and menthol, while TRPV1 is activated by heat and capsaicin.

Dysregulation of TRPM channels has been implicated in various pathological conditions, including pain, neurodegenerative diseases, and cancer. Therefore, understanding the structure and function of these channels may provide insights into potential therapeutic targets for these conditions.

NAV1.5, also known as SCN5A, is a specific type of voltage-gated sodium channel found in the heart muscle cells (cardiomyocytes). These channels play a crucial role in the generation and transmission of electrical signals that coordinate the contraction of the heart.

More specifically, NAV1.5 channels are responsible for the rapid influx of sodium ions into cardiomyocytes during the initial phase of the action potential, which is the electrical excitation of the cell. This rapid influx of sodium ions helps to initiate and propagate the action potential throughout the heart muscle, allowing for coordinated contraction and proper heart function.

Mutations in the SCN5A gene, which encodes the NAV1.5 channel, have been associated with various cardiac arrhythmias, including long QT syndrome, Brugada syndrome, and familial atrial fibrillation, among others. These genetic disorders can lead to abnormal heart rhythms, syncope, and in some cases, sudden cardiac death.

Biotinyllation is a process of introducing biotin (a vitamin) into a molecule, such as a protein or nucleic acid (DNA or RNA), through chemical reaction. This modification allows the labeled molecule to be easily detected and isolated using streptavidin-biotin interaction, which has one of the strongest non-covalent bonds in nature. Biotinylated molecules are widely used in various research applications such as protein-protein interaction studies, immunohistochemistry, and blotting techniques.

Voltage-gated potassium channels are a type of ion channel found in the membrane of excitable cells such as nerve and muscle cells. They are called "voltage-gated" because their opening and closing is regulated by the voltage, or electrical potential, across the cell membrane. Specifically, these channels are activated when the membrane potential becomes more positive, a condition that occurs during the action potential of a neuron or muscle fiber.

When voltage-gated potassium channels open, they allow potassium ions (K+) to flow out of the cell down their electrochemical gradient. This outward flow of K+ ions helps to repolarize the membrane, bringing it back to its resting potential after an action potential has occurred. The precise timing and duration of the opening and closing of voltage-gated potassium channels is critical for the normal functioning of excitable cells, and abnormalities in these channels have been linked to a variety of diseases, including cardiac arrhythmias, epilepsy, and neurological disorders.

Cyclic AMP (cAMP)-dependent protein kinases, also known as protein kinase A (PKA), are a family of enzymes that play a crucial role in intracellular signaling pathways. These enzymes are responsible for the regulation of various cellular processes, including metabolism, gene expression, and cell growth and differentiation.

PKA is composed of two regulatory subunits and two catalytic subunits. When cAMP binds to the regulatory subunits, it causes a conformational change that leads to the dissociation of the catalytic subunits. The freed catalytic subunits then phosphorylate specific serine and threonine residues on target proteins, thereby modulating their activity.

The cAMP-dependent protein kinases are activated in response to a variety of extracellular signals, such as hormones and neurotransmitters, that bind to G protein-coupled receptors (GPCRs) or receptor tyrosine kinases (RTKs). These signals lead to the activation of adenylyl cyclase, which catalyzes the conversion of ATP to cAMP. The resulting increase in intracellular cAMP levels triggers the activation of PKA and the downstream phosphorylation of target proteins.

Overall, cAMP-dependent protein kinases are essential regulators of many fundamental cellular processes and play a critical role in maintaining normal physiology and homeostasis. Dysregulation of these enzymes has been implicated in various diseases, including cancer, diabetes, and neurological disorders.

An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

GTP-binding protein alpha subunits, Gq-G11, are a family of heterotrimeric G proteins that play a crucial role in intracellular signaling transduction pathways. They are composed of three subunits: alpha, beta, and gamma. The alpha subunit of this family is referred to as Gαq, Gα11, Gα14, or Gα15/16, depending on the specific type.

These G proteins are activated by G protein-coupled receptors (GPCRs) upon binding of an agonist to the receptor. The activation leads to the exchange of GDP for GTP on the alpha subunit, causing it to dissociate from the beta and gamma subunits and further interact with downstream effector proteins. This interaction ultimately results in the activation of various signaling cascades, including the phospholipase C beta (PLCβ) pathway, which leads to the production of second messengers such as inositol trisphosphate (IP3) and diacylglycerol (DAG), and subsequently calcium mobilization.

Defects or mutations in GTP-binding protein alpha subunits, Gq-G11, have been implicated in several diseases, such as cancer, cardiovascular disorders, and neurological conditions.

Lymphocyte Antigen 96 (LY96), also known as MD-1 or myeloid differentiation factor 1, is a protein that is primarily expressed on the surface of B cells and some types of antigen-presenting cells. It associates with CD14/TLR4/MD-2 complex and plays an important role in the recognition and response to lipopolysaccharides (LPS) found on gram-negative bacteria. LY96 is involved in the activation of signaling pathways that lead to the production of pro-inflammatory cytokines, which are crucial for the immune response against bacterial infections.

CHO cells, or Chinese Hamster Ovary cells, are a type of immortalized cell line that are commonly used in scientific research and biotechnology. They were originally derived from the ovaries of a female Chinese hamster (Cricetulus griseus) in the 1950s.

CHO cells have several characteristics that make them useful for laboratory experiments. They can grow and divide indefinitely under appropriate conditions, which allows researchers to culture large quantities of them for study. Additionally, CHO cells are capable of expressing high levels of recombinant proteins, making them a popular choice for the production of therapeutic drugs, vaccines, and other biologics.

In particular, CHO cells have become a workhorse in the field of biotherapeutics, with many approved monoclonal antibody-based therapies being produced using these cells. The ability to genetically modify CHO cells through various methods has further expanded their utility in research and industrial applications.

It is important to note that while CHO cells are widely used in scientific research, they may not always accurately represent human cell behavior or respond to drugs and other compounds in the same way as human cells do. Therefore, results obtained using CHO cells should be validated in more relevant systems when possible.

Calcium signaling is the process by which cells regulate various functions through changes in intracellular calcium ion concentrations. Calcium ions (Ca^2+^) are crucial second messengers that play a critical role in many cellular processes, including muscle contraction, neurotransmitter release, gene expression, and programmed cell death (apoptosis).

Intracellular calcium levels are tightly regulated by a complex network of channels, pumps, and exchangers located on the plasma membrane and intracellular organelles such as the endoplasmic reticulum (ER) and mitochondria. These proteins control the influx, efflux, and storage of calcium ions within the cell.

Calcium signaling is initiated when an external signal, such as a hormone or neurotransmitter, binds to a specific receptor on the plasma membrane. This interaction triggers the opening of ion channels, allowing extracellular Ca^2+^ to flow into the cytoplasm. In some cases, this influx of calcium ions is sufficient to activate downstream targets directly. However, in most instances, the increase in intracellular Ca^2+^ serves as a trigger for the release of additional calcium from internal stores, such as the ER.

The release of calcium from the ER is mediated by ryanodine receptors (RyRs) and inositol trisphosphate receptors (IP3Rs), which are activated by specific second messengers generated in response to the initial external signal. The activation of these channels leads to a rapid increase in cytoplasmic Ca^2+^, creating a transient intracellular calcium signal known as a "calcium spark" or "calcium puff."

These localized increases in calcium concentration can then propagate throughout the cell as waves of elevated calcium, allowing for the spatial and temporal coordination of various cellular responses. The duration and amplitude of these calcium signals are finely tuned by the interplay between calcium-binding proteins, pumps, and exchangers, ensuring that appropriate responses are elicited in a controlled manner.

Dysregulation of intracellular calcium signaling has been implicated in numerous pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. Therefore, understanding the molecular mechanisms governing calcium homeostasis and signaling is crucial for the development of novel therapeutic strategies targeting these diseases.

GTP-binding proteins, also known as G proteins, are a family of molecular switches present in many organisms, including humans. They play a crucial role in signal transduction pathways, particularly those involved in cellular responses to external stimuli such as hormones, neurotransmitters, and sensory signals like light and odorants.

G proteins are composed of three subunits: α, β, and γ. The α-subunit binds GTP (guanosine triphosphate) and acts as the active component of the complex. When a G protein-coupled receptor (GPCR) is activated by an external signal, it triggers a conformational change in the associated G protein, allowing the α-subunit to exchange GDP (guanosine diphosphate) for GTP. This activation leads to dissociation of the G protein complex into the GTP-bound α-subunit and the βγ-subunit pair. Both the α-GTP and βγ subunits can then interact with downstream effectors, such as enzymes or ion channels, to propagate and amplify the signal within the cell.

The intrinsic GTPase activity of the α-subunit eventually hydrolyzes the bound GTP to GDP, which leads to re-association of the α and βγ subunits and termination of the signal. This cycle of activation and inactivation makes G proteins versatile signaling elements that can respond quickly and precisely to changing environmental conditions.

Defects in G protein-mediated signaling pathways have been implicated in various diseases, including cancer, neurological disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of GTP-binding proteins is essential for developing targeted therapeutic strategies.

A missense mutation is a type of point mutation in which a single nucleotide change results in the substitution of a different amino acid in the protein that is encoded by the affected gene. This occurs when the altered codon (a sequence of three nucleotides that corresponds to a specific amino acid) specifies a different amino acid than the original one. The function and/or stability of the resulting protein may be affected, depending on the type and location of the missense mutation. Missense mutations can have various effects, ranging from benign to severe, depending on the importance of the changed amino acid for the protein's structure or function.

The Kv1.5 potassium channel, also known as KCNA5, is a type of voltage-gated potassium channel that is widely expressed in various tissues, including the heart and blood vessels. It plays a crucial role in regulating electrical excitability and maintaining physiological functions in these tissues.

In the heart, Kv1.5 channels are primarily located in the atria and contribute to the repolarization phase of the cardiac action potential. They help establish the rapid delayed rectifier current (IKr), which is essential for normal atrial electrical activity and maintaining proper heart rhythm. Mutations or dysfunctions in Kv1.5 channels can lead to various cardiac arrhythmias, such as atrial fibrillation.

In blood vessels, Kv1.5 channels are involved in the regulation of vascular tone and blood pressure. They contribute to the hyperpolarization of vascular smooth muscle cells, which leads to vasodilation and decreased peripheral resistance. Dysregulation of Kv1.5 channels has been implicated in several cardiovascular diseases, including hypertension and atherosclerosis.

Overall, Kv1.5 potassium channels are critical for maintaining proper electrical activity in the heart and regulating vascular tone, making them an important target for therapeutic interventions in various cardiovascular disorders.

Cricetinae is a subfamily of rodents that includes hamsters, gerbils, and relatives. These small mammals are characterized by having short limbs, compact bodies, and cheek pouches for storing food. They are native to various parts of the world, particularly in Europe, Asia, and Africa. Some species are popular pets due to their small size, easy care, and friendly nature. In a medical context, understanding the biology and behavior of Cricetinae species can be important for individuals who keep them as pets or for researchers studying their physiology.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

Toll-like receptor 2 (TLR2) is a type of protein belonging to the family of pattern recognition receptors (PRRs), which play a crucial role in the innate immune system's response to pathogens. TLR2 is primarily expressed on the surface of various immune cells, including monocytes, macrophages, dendritic cells, and B cells.

TLR2 recognizes a wide range of microbial components, such as lipopeptides, lipoteichoic acid, and zymosan, derived from both gram-positive and gram-negative bacteria, fungi, and certain viruses. Upon recognition and binding to these ligands, TLR2 initiates a signaling cascade that activates various transcription factors, leading to the production of proinflammatory cytokines, chemokines, and costimulatory molecules. This response is essential for the activation and recruitment of immune cells to the site of infection, thereby contributing to the clearance of invading pathogens.

In summary, TLR2 is a vital pattern recognition receptor that helps the innate immune system detect and respond to various microbial threats by initiating an inflammatory response upon ligand binding.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.

As a consequence, HEK 293 cells should not be used as an in vitro model of typical kidney cells. HEK 293 cells have a complex ... HEK 293 Transfection and Selection Data @ Cell-culture Database A HEK293 Cell Database 293 Cells (CRL-1573) Archived 2012-06-22 ... Human embryonic kidney 293 cells, also often referred to as HEK 293, HEK-293, 293 cells, or less precisely as HEK cells, are a ... They are quite similar to each other but show detectable divergence from the parental HEK 293 cell line. HEK 293 cells are ...
With Graham's contributions in transfection of the cells with the adenovirus 5 this led to the cell line of HEK 293 cells. HEK ... "HEK293 Cell Line". hek293.com. Archived from the original on 16 October 2014. "In memoriam professor Mathieu Noteborn" (in ... he created the PER.C6 cell line with enhanced traceability compared to the HEK 293 line, this time coming from retinal cells. ... In contrast to HEK 293 the PER.C6 cell line was patented by Leiden University and IntroGene (later Crucell) and used ...
This was verified using GPR18 transfected HEK-293 cells. The same migration wasn't witnessed using non-transfected and GPR55 ... NAGly has been hypothesized to induce cell migration in BV-2 microglia cells. The same research suggests that this migration ... NAGly powerfully stimulates oxygen consumption in multiple cell lines, including murine C2C12 myoblasts and human HEK293T cells ... Cell. 166 (2): 424-435. doi:10.1016/j.cell.2016.05.071. PMC 4947008. PMID 27374330. Lin H, Long JZ, Roche AM, Svensson KJ, Dou ...
2007). "Upregulation of PHLDA2 in Dicer knockdown HEK293 cells". Biochim. Biophys. Acta. 1770 (5): 820-5. doi:10.1016/j.bbagen. ...
"Subcellular localization of human neutral ceramidase expressed in HEK293 cells". Biochemical and Biophysical Research ...
2005). "Subcellular localization of human neutral ceramidase expressed in HEK293 cells". Biochem. Biophys. Res. Commun. 331 (1 ... 2006). "Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P". ...
"The CAG promoter maintains high-level transgene expression in HEK293 cells". FEBS Open Bio. 11 (1): 95-104. doi:10.1002/2211- ... Okabe M, Ikawa M, Kominami K, Nakanishi T, Nishimune Y (May 1997). "'Green mice' as a source of ubiquitous green cells". FEBS ... BMC Cell Biology. 9: 2. doi:10.1186/1471-2121-9-2. PMC 2254385. PMID 18190688. Miyazaki J, Takaki S, Araki K, Tashiro F, ... promoter can be used to drive transgene expression during the differentiation of murine embryonic stem cells into vascular ...
However, the HEK 293 cells used for vaccine manufacturing, express several adenoviral genes, including the ones required for ... To manufacture the vaccine the virus is propagated on HEK 293 cell lines and then purified multiple times to completely remove ... Thomas P, Smart TG (2005). "HEK293 cell line: a vehicle for the expression of recombinant proteins". J Pharmacol Toxicol ... Cell Research. 18 (2): 290-301. doi:10.1038/cr.2008.15. PMC 7091891. PMID 18227861. "There are no foetal cells in the ...
Both Ad26 and Ad5 were modified to remove the E1 gene to prevent replication outside the HEK 293 cells. For the production of ... Rarely, Ad5 can acquire the E1 gene from the HEK 293 cells, restoring its ability to replicate. Gamaleya has set an acceptable ... Tan E, Chin CS, Lim ZF, Ng SK (2021). "HEK293 Cell Line as a Platform to Produce Recombinant Proteins and Viral Vectors". ... Large quantities of both adenoviruses are produced by HEK 293 cells that have the E1 gene necessary for viral replication. ...
"Functional comparison of HCN isoforms expressed in ventricular and HEK 293 cells". Pflügers Archiv. 444 (5): 597-601. doi: ...
The virus is grown in HEK 293 cells and purified for administration. It was developed by Spark Therapeutics and Children's ... due to inherited retinal dystrophy caused by confirmed biallelic RPE65 mutations and who have sufficient viable retinal cells. ...
Knock down of SIRT7 in HEK293 cells resulted in decreased rRNA levels. This same study found that this SIRT3 knockdown ... In humans cells, SIRT7 has only been shown to interact with two other molecules: RNA polymerase I (RNA Pol I) and upstream ... Mohrin M, Shin J, Liu Y, Brown K, Luo H, Xi Y, Haynes CM, Chen D (Mar 2015). "Stem cell aging. A mitochondrial UPR-mediated ... Sun L, Dang W (July 2020). "SIRT7 slows down stem cell aging by preserving heterochromatin: a perspective on the new discovery ...
"Functional comparison of HCN isoforms expressed in ventricular and HEK 293 cells". Pflügers Archiv. 444 (5): 597-601. doi: ... Calloe K, Elmedyb P, Olesen SP, Jorgensen NK, Grunnet M (Sep 2005). "Hypoosmotic cell swelling as a novel mechanism for ... Cell. 93 (5): 717-29. doi:10.1016/S0092-8674(00)81434-8. PMID 9630217. S2CID 10265917. Hofmann F, Biel M, Kaupp UB (Dec 2005 ... "Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization". ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. ... "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells". Mol. Med. 8 (2): 95- ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... Cell. 122 (6): 957-68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923. Guo D ... "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". ... 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ...
2006). "Acute hypoxic regulation of recombinant THIK-1 stably expressed in HEK293 cells". Adv. Exp. Med. Biol. ADVANCES IN ... 2008). "Cellular localization of THIK-1 (K(2P)13.1) and THIK-2 (K(2P)12.1) K channels in the mammalian kidney". Cell. Physiol. ...
December 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and ...
December 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and ... in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells". Molecular and Cellular Biology ... "Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines". Oncogene. 17 (10): ... Cell. 96 (5): 645-53. doi:10.1016/S0092-8674(00)80575-9. PMID 10089880. S2CID 17117789. Deng L, Wang C, Spencer E, Yang L, ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... Cell. 122 (6): 957-68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923. Rual ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. ... Cell. Biol. 20 (9): 3157-67. doi:10.1128/MCB.20.9.3157-3167.2000. PMC 85610. PMID 10757800. Zhang QH, Ye M, Wu XY, Ren SX, Zhao ... Cell. Biol. 20 (9): 3157-67. doi:10.1128/mcb.20.9.3157-3167.2000. PMC 85610. PMID 10757800. Datta PK, Chytil A, Gorska AE, ... "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621-5. doi:10.1126/science. ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... Molecular Cell. 5 (5): 779-87. doi:10.1016/S1097-2765(00)80318-4. PMID 10882114. Will CL, Schneider C, MacMillan AM, Katopodis ... "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94-101. doi:10.1038/ ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. ... "Specific association of estrogen receptor beta with the cell cycle spindle assembly checkpoint protein, MAD2". Proc. Natl. Acad ... "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94-101. doi:10.1038/nbt1046. ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. ... "Identification of candidate radioresistant genes in human squamous cell carcinoma cells through gene expression analysis using ... Cell Biol. 6 (2): 97-105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986. Higo M, Uzawa K, Kouzu Y, Bukawa H, Nimura Y, ... Cell. Proteomics. 4 (11): 1725-40. doi:10.1074/mcp.M500231-MCP200. PMID 16085932. Human CCT6A genome location and CCT6A gene ...
"Synthetic ciguatoxins selectively activate Nav1.8-derived chimeric sodium channels expressed in HEK293 cells". The Journal of ... Voltage clamp has been used to show how action potentials in DRG cells are shaped by TTX-resistant sodium channels. Nav1.8 ... Lipid rafts organise the cell membrane, which includes trafficking and localising ion channels. Removal of lipid rafts in the ... Although NaV1.8 is not normally expressed within the cerebellum, its expression is up-regulated in cerebellar Purkinje cells in ...
December 2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and ... Within cells, IDH1 has been observed to localize to the cytoplasm, peroxisome, and endoplasmic reticulum. Under hypoxic ... In addition, IDH1 is key to β-oxidation of unsaturated fatty acids in the peroxisomes of liver cells. IDH1 also participates in ... Vaccination of MHC-humanized transgenic mice with mutant IDH1 peptide induced an IFN-γ CD4+ T-helper 1 cell response, ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... "The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus of proliferating cells". Molecular Biology of the Cell. 9 ... "Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells". The Journal of Cell Biology. 143 (6): ... Gangwani L (December 2006). "Deficiency of the zinc finger protein ZPR1 causes defects in transcription and cell cycle ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... IDH3 activity is regulated by the energy needs of the cell: when the cell requires energy, IDH3 is activated by ADP; and when ... Within cells, IDH3 and its subunits have been observed to localize to the mitochondria. IDH3α expression has been linked to ... HIF-1 is largely known for shifting glucose metabolism from oxidative phosphorylation to aerobic glycolysis in cancer cells ( ...
"Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical ... "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". ... 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell ...
2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. ... 2008). "Direct role of nucleotide metabolism in C-MYC-dependent proliferation of melanoma cells". Cell Cycle. 7 (15): 2392-400 ... 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685. He Y, Mou Z, Li W, et al. (2009). "Identification of IMPDH2 as a ...
As a consequence, HEK 293 cells should not be used as an in vitro model of typical kidney cells. HEK 293 cells have a complex ... HEK 293 Transfection and Selection Data @ Cell-culture Database A HEK293 Cell Database 293 Cells (CRL-1573) Archived 2012-06-22 ... Human embryonic kidney 293 cells, also often referred to as HEK 293, HEK-293, 293 cells, or less precisely as HEK cells, are a ... They are quite similar to each other but show detectable divergence from the parental HEK 293 cell line. HEK 293 cells are ...
HEK 293 cells, SIL MS Protein Standard, 13C- and 15N-labeled; ApoA-1 (apolipoprotein A-1) is a 29; ... recombinant, expressed in HEK 293 cells, SIL MS Protein Standard, 13C- and 15N-labeled. ... Cell Culture & Analysis. Chemistry & Biochemicals. Clinical & Diagnostics. Filtration. Greener Alternative Products. Industrial ... Cell Culture & Analysis. Chemistry & Synthesis Clinical & Diagnostics. Environmental & Cannabis Testing. Food & Beverage ...
HEK293) cell line with sulfation capacities. We stably engineered O-glycan sulfation capacities in HEK293 cells by site- ... HEK293) cell line with sulfation capacities. We stably engineered O-glycan sulfation capacities in HEK293 cells by site- ... Expression of the galactose 3-O-sulfotransferase 2 in HEK293 cells resulted in sulfation of core1 and core2 O-glycans, whereas ... Expression of the galactose 3-O-sulfotransferase 2 in HEK293 cells resulted in sulfation of core1 and core2 O-glycans, whereas ...
Effects of 31 herbal formulae on hERG potassium channel activity in the voltage-clamp assay using HEK 293 cells. Concentration- ... 2019; Cardiac safety assessment of medicinal herbal formulas using hERG-HEK 293 cell. Journal of Korean Medicine. 40:2. 94-105 ... Cardiotoxicity assessment of 31 herbal formulae by activity of hERG potassium channel in HEK 293 cells. ... Cardiac Safety Assessment of Medicinal Herbal Formulas Using hERG-HEK 293 cell 2019 ;40(2). ...
Specific, live-cell detection of extracellular expressed or secreted proteins. ... Quantify HiBiT-tagged proteins expressed on the cell surface. ... HEK293 LgBiT Cell Line and LgBiT Expression Vector. Reagents ... Internalization of HiBiT-ADRB2 in stably transfected HEK293 cells in 384-well plates ... Quantify HiBiT-Tagged Proteins Expressed on the Cell Surface. *Specific, live-cell detection of extracellular expressed or ...
HEK293 Cells * Heredity * Humans * Iodide Peroxidase / genetics* * Iodide Peroxidase / metabolism * Kinetics * Male ...
GFAP is also found in the lens epithelium, Kupffer cells of the liver, in some cells in salivary tumors and has been reported ... In addition, neural stem cells strongly express GFAP. Antibodies to GFAP are very useful as markers of astrocytic cells. In ... Bergmann glial cell differentiation positive regulation of glial cell proliferation long-term synaptic potentiation regulation ... in satellite cells of peripheral ganglia, and in non-myelinating Schwann cells of peripheral nerves. ...
... human osteosarcoma U2OS cell line] and HEK293 [Human Embryonic Kidney 293 cell] cells were grown in DMEM/5% with Pen/Strep.. ... Translation initiation rate on Kif18b reporter in U2OS and HEK293 cells. Range. 1.4-3.6 min^−1 ... Cell. 2016 May 5 165(4):976-89. doi: 10.1016/j.cell.2016.04.034. p.980 left column top paragraphPubMed ID27153498 ... Time of mRNA translocation from the nucleus, mRNA diffusion coefficient & translocation velocity in human U2OS cells. ...
Crystallography grade LSM12B Origin: Human Host: Insect Cells Recombinant ,95 % as determined by SDS PAGE, Size Exclusion ... HEK-293 Cells Validations *(1). Cat. No. ABIN2724978 Quantity 20 μg ...
Comparison of cell proliferation rate and cell morphology. HEK 293 and CHO cells were cultured using both this product and ... Proliferation curves and cell morphology of HEK 293 cells cultured under various serum concentrations (Day 35). Proliferation ... In comparison to DMEM / Hams F-12 medium, this product allows for cell cultivation with reduced serum supplementation, without ... We prepared droplets (n=4) embedding dispersed colon cancer patient-derived organoid cells using Corning® Matrigel Basement ...
Cyclin I is a specific binding partner and activator of Cdk5 in HEK293 cells. (A) Following cotransfection of HEK293 cells with ... Cell culture. HEK293 cells (ATCC) were cultured under standard conditions at 37°C in DMEM media (Invitrogen). Conditionally ... CDK inhibitors: cell cycle regulators and beyond. Dev. Cell. 14:159-169. View this article via: CrossRef PubMed Google Scholar ... Figure 2, B and C, shows that in transfected HEK293 cells, the cyclin I-Cdk5 complex alone was able to phosphorylate histone H1 ...
The ZnHApD solution presented a non-toxic activity against HEK-293 cells for all analyzed concentrations. The antibacterial ... The cell growth and toxicity of HEK-293 cells were investigated on the ZnHApD solution for four different concentrations and ... The HEK-293 cells were seeded on 6-well plates (5 × 105 cells/well). When cells had adhered to the plates, the medium was ... The cell growth and toxicity of HEK-293 cells were investigated on the ZnHApD solution for four different concentrations and ...
Lane 1 : Wild-type HEK-293 cell lysate. Lane 2 : PDCD6IP knockout HEK-293 cell lysate. Lane 3 : HeLa cell lysate. Lane 4 : ... whole cell lysate. Lane 5 : MCF7 (human breast adenocarcinoma epithelial cell) whole cell lysate. Lane 6 : Jurkat (human T cell ... Lane 2 : HEK-293 (human embryonic kidney epithelial cell) whole cell lysate. Lane 3 : HeLa (human cervix adenocarcinoma ... ICC/IF: NIH/3T3 and HeLa cells. Flow Cyt (intra): NIH/3T3 and HeLa cells. IP: K562 whole cell lysate. ...
Full length human recombinant protein of human DPP3(NP_005691) produced in HEK293 cell.. ...
Cell culture and transient transfection of N2A and HEK293. Human embryonal kidney cells (HEK293) (DSMZ no.: ACC 305) and murine ... To exclude cell line-specific effects, we additionally used HEK293 cells and over-expressed GGA1, 2 or 3 together with S1 and ... Figure 1. GGAs alter α-synuclein oligomer secretion in N2A cells. N2A cells were co-transfected with α-syn fused to non- ... HEK293 and N2A cells were seeded in 12 or 24 well plate formats as described above. Then, 48h after transient transfection with ...
Neuro-2a cells, SGC-7901 cells, mouse brain tissue, HEK-293 cells, mouse heart tissue, rat heart tissue. ... WB analysis of HEK-293 using 15287-1-AP. HEK-293 cells were subjected to SDS PAGE followed by western blot with 15287-1-AP ( ... WB analysis of HEK-293 using 15287-1-AP. HEK-293 cells were subjected to SDS PAGE followed by western blot with 15287-1-AP ( ... IF Staining of HEK-293 using 15287-1-AP. Immunofluorescent analysis of (10% Formaldehyde) fixed HEK-293 cells using 15287-1-AP ...
DNA Damage Signaling Is Required for Replication of Human Bocavirus 1 DNA in Dividing HEK293 Cells. J Virol. 2017 Jan 1. 91 (1 ... Lindner J, Zehentmeier S, Franssila R, Barabas S, Schroeder J, Deml L. CD4+ T helper cell responses against human bocavirus ... Epidemiologic and Clinical Characteristics of Coronavirus and Bocavirus Respiratory Infections after Allogeneic Stem Cell ...
Cell culture and transfection. Request a detailed protocol HEK293 and NIH3T3 cells were cultured in DMEM (HyClone, South Logan ... Transfected HEK293 cells were lysed in 1X ELB lysis buffer supplemented with 2 mM NaPPi, 10 mM NaF, 2 mM Na3VO4, 1 mM DTT, and ... Transfected HEK293 cells were lysed in actin fractionation buffer (10 mM Tris pH 7.4, 2 mM MgCl2, 1% Triton X-100, 0.2 mM DTT, ... Transfected HEK293 cells were lysed in 1X ELB lysis buffer and were IPed with FLAG antibody and protein-A agarose beads to ...
However, shikonin inhibited neither RANTES nor MIP-1alpha binding to CCR5 transfected HEK/293 cells [16]. ... HEK)/293 cells with IC50 values of 2.63 x 10(-6) and 2.57 x 10(-6) M, respectively [16]. ... we showed that the administration of shikonin could result in the induction of apoptotic cell death of human hepatoma cell line ... most efficiently induced cell-death in two lines of lung cancer cells, namely, NCI-H522 and DMS114, whereas shikonin was ...
A comparable previous study investigating HEK293 cells transfected with human APJ also identified ERK1/2 induction by apelin ( ... In a previous study, apelin was not detected in glial cells in clinical and rat epilepsy models (32). In mice with amyotrophic ... Apelin-13 is the strongest APJ activator expressed in cells (3,15). As an adipocytokine, apelin is expressed in and secreted by ... CCI induced a marked increase in APJ expression and an increased number of APJ-immunoreactive cells was observed in the CCI ...
HEK 293 cells are used for transient production and CHO cells are used as the stable cell line. When you switch expression ... "By introducing the large T-antigen of the SV40 virus into our CAP cells, we generated our CAP-T cells, a cell line optimized ... "CAP cells are designed for stable protein production, so you have to put the cells under selection pressure and go through a ... CAP Cells. Cevec Pharmaceuticals protein and vaccine production work is based on its CAP cell line of immortalized human ...
Furthermore, HEK293 reporter cell lines were employed to evaluate the role of Toll-like receptor activation. Notably, SWCNT ... First, we determined the endotoxin content of all the materials, a prerequisite for any studies using immune-competent cells. ... Using THP-1 knockdown cell lines, we found that IL-1beta secretion was caspase-1-, ASC-, and NLRP3- dependent. ... Cell signaling; Microorganisms; Cytokines; Single-walled carbon nanotubes; SWCNT; Humans; Macrophages; Endotoxins; Cytotoxicity ...
HeLa cells were cultured in DMEM supplemented with 10% calf serum, and HEK-293 cells were cultured in DMEM supplemented with 5 ... HeLa cell extract was used instead of HEK-293S cells. Similar to HEK-293S cells, HeLa cells do not support 5HT3R reporter ... By contrast, no significant reporter activity was seen in human embryonic kidney HEK-293 (Fig. 3B) or HeLa cells (data not ... Cell culture and transfection studies. N18-TG2 cells were cultured in DMEM supplemented with 10% fetal calf serum (FCS), 60 nm ...
MULAN laxogenin siRNA transfection led to the inhibition of Akt ubiquitination in HEK293 cells (Body 2D left -panel). Oddly ... After transfection with plasmids as indicated HEK293 cells … The ability to generate diverse substrate-ubiquitin structures is ... Similarly MULAN-induced Akt degradation preferentially occurred in serum-stimulated HEK293 cells (Physique 3B). In addition ... To address this an ubiquitination assay was performed in HeLa cells expressing HA-tagged ubiquitin in which lysine 48 or 63 was ...
... fusion protein stably expressed in HEK293 cells; functional significance and correlation with biophysical state of plasma ... Kavan, L; Marcaccio, M; Paolucci, F; Exploiting Nanocarbons in Dye-Sensitized Solar Cells; Top. Curr. Chem.; 2014 348 53-93 ... Chippendale, TWE; Spanel, P; Smith, D; El Haj, AJ; Counting cell number in situ by quantification of dimethyl sulphide in ... Kavan, L; Liska, P; Zakeeruddin, SM; Gratzel, M; Optically Transparent FTO-Free Cathode for Dye-Sensitized Solar Cells; ACS ...
... and recombinant full-length human HE4 expressed in HEK 293 cells (Abcam, Cambridge, MA, cat #ab152016). ... Human antigen grade CA125 purified from an ovarian cancer cell line (Meridian Life Sciences Inc, Memphis, TN, cat # A97180H), ... human antigen grade CA15.3 derived from human breast cancer BTA cell line supernatant (Meridian, cat # A32000H), ...
IL-4R alpha/CD124, Human (M26-Q231) is produced in HEK293 cells with a C-Terminal mFc-tag. MedChemExpress offers high purity IL ... inhibits IL4-mediated cell proliferation and IL-5 up-regulation by T-cells. ... alpha/CD124 Protein, Human (HEK293, mFc) with excellent lot-to-lot consistency, superior biological activity and low endotoxin ... IL-4R alpha/CD124, Human (M26-Q231) is produced in HEK293 cells with a C-Terminal mFc-tag. ...
G-protein-coupled visits and endogenous response in longitudinal cells for recombinant and first HEK293-6E. cell-based analyses ... long-term cells for smooth genes. The precession is of each smoother are Now such to the 6th models when the producer data ... penalized cell is the approach of covariates on a site. In this precession, a target content has 10 amplification in use( the ... The molecular two cells are Markov precession nutation and wobble of the earth Monte Carlo( MCMC) plates to characterize the ...
... the UpTempo AAV platform was expanded in March of 2023 to include Catalents own HEK293 producer cell line and off-the-shelf ... clonal HEK293 cell line, and off-the-shelf plasmids to support a robust supply chain. ... will detail the integrated services within the UpTempo AAV development platform and the use of standardised protocols for cell ...
  • Human embryonic kidney 293 cells, also often referred to as HEK 293, HEK-293, 293 cells, or less precisely as HEK cells, are a specific immortalised cell line derived from a spontaneously miscarried or aborted fetus or human embryonic kidney cells grown in tissue culture taken from a female fetus in 1973. (wikipedia.org)
  • To explore further the genetic and biosynthetic regulation of sulfated O-glycans, here we expanded a cell-based glycan array in the human embryonic kidney 293 (HEK293) cell line with sulfation capacities. (lu.se)
  • P.987 left column bottom paragraph: 'U2OS [human osteosarcoma U2OS cell line] and HEK293 [Human Embryonic Kidney 293 cell] cells were grown in DMEM/5% with Pen/Strep. (harvard.edu)
  • HEK 293 cells have been widely used in cell biology research for many years, because of their reliable growth and propensity for transfection. (wikipedia.org)
  • HEK 293 cells were generated in 1973 by transfection of cultures of normal human embryonic kidney cells with sheared adenovirus 5 DNA in Alex van der Eb's laboratory in Leiden, the Netherlands. (wikipedia.org)
  • Graham performed the transfection a total of eight times, obtaining just one clone of cells that were cultured for several months. (wikipedia.org)
  • Surprisingly, mutation of the NF1 binding site abolished all reporter activity in cell transfection studies, suggesting that this element is essential for neuronal-specific transcriptional activity of the 5HT 3 R. Furthermore, a complex of neuronal proteins that includes a member(s) of the NF1 family binds to this site, as shown by gel mobility super shift and DNaseI footprinting analyses. (jneurosci.org)
  • MULAN laxogenin siRNA transfection led to the inhibition of Akt ubiquitination in HEK293 cells (Body 2D left -panel). (bioskinrevive.com)
  • After transfection with plasmids as indicated HEK293 cells … The ability to generate diverse substrate-ubiquitin structures is usually important for targeting proteins to different fates 28. (bioskinrevive.com)
  • In her talk, Dr Connolly will detail the integrated services within the UpTempo AAV development platform and the use of standardised protocols for cell culture, transfection, and downstream purification to save time, as well as the advantages it now has with an in-house, clonal HEK293 cell line, and off-the-shelf plasmids to support a robust supply chain. (manufacturingchemist.com)
  • Originally launched in 2022, the UpTempo AAV platform was expanded in March of 2023 to include Catalent's own HEK293 producer cell line and off-the-shelf plasmids, including pHelper and rep/cap. (manufacturingchemist.com)
  • Furthermore, HEK293 reporter cell lines were employed to evaluate the role of Toll-like receptor activation. (cdc.gov)
  • Here, we use a human cell-based reporter assay to characterize off- target cleavage of Cas9-based RGENs. (cdc.gov)
  • Graham and coworkers provided evidence that HEK 293 cells and other human cell lines generated by adenovirus transformation of human embryonic kidney cells have many properties of immature neurons, suggesting that the adenovirus preferentially transformed a neuronal lineage cell in the original kidney culture. (wikipedia.org)
  • Given the location of the adrenal gland (adrenal means "next to the kidney"), a few adrenal cells could plausibly have appeared in an embryonic kidney derived culture, and could be preferentially transformed by adenovirus. (wikipedia.org)
  • Similarly MULAN-induced Akt degradation preferentially occurred in serum-stimulated HEK293 cells (Physique 3B). (bioskinrevive.com)
  • 293T (or HEK 293T) is a derivative human cell line that expresses a mutant version of the SV40 large T antigen. (wikipedia.org)
  • A comprehensive study of the genomes and transcriptomes of HEK 293 and five derivative cell lines compared the HEK 293 transcriptome with that of human kidney, adrenal, pituitary and central nervous tissue. (wikipedia.org)
  • Adenoviruses transform neuronal lineage cells much more efficiently than typical human kidney epithelial cells. (wikipedia.org)
  • Expressed in human 293 cells, it is designed to be used as an internal standard for bioanalysis of ApoA1 in mass-spectrometry. (sigmaaldrich.com)
  • Full length human recombinant protein of human DPP3(NP_005691) produced in HEK293 cell. (origene.com)
  • In line with this, α-syn oligomers were found in conditioned media from cell cultures as well as human CSF and plasma [ 27 - 30 ]. (aging-us.com)
  • Cevec Pharmaceuticals' protein and vaccine production work is based on its CAP cell line of immortalized human amniocytes, which are especially useful for ensuring that human proteins receive post-translational modifications correctly and efficiently-via glycosylation, for example. (genengnews.com)
  • with small or large lateral dimensions) are sensed by primary human macrophages which are key cells of the innate immune system. (cdc.gov)
  • IL-4R alpha/CD124 , Human (M26-Q231) is produced in HEK293 cells with a C-Terminal mFc-tag. (medchemexpress.com)
  • We readily detected off-target alterations induced by four out of six RGENs targeted to endogenous loci in human cells by examination of partially mismatched sites. (cdc.gov)
  • Our work demonstrates that RGENs are highly active even with imperfectly matched RNA-DNA interfaces in human cells, a finding that might confound their use in research and therapeutic applications. (cdc.gov)
  • Recent work has demonstrated that clustered, regularly interspaced, short palindromic repeats (CRISPR)/CRISPR-associated (Cas) systems1-3 can serve as the basis of a simple and highly efficient method for performing genome editing in bacteria, yeast and human cells, as well as in vivo in whole organisms such as fruit flies, zebrafish and mice4-13. (cdc.gov)
  • Although Maraffini and colleagues7 recently performed a systematic investigation of Cas9 RGEN specificity in bacteria, the specificities of RGENs in human cells have not been extensively defined and, to our knowledge, bona fide off-target mutations induced by Cas9 have not been identified in any eukaryotic cell or organism. (cdc.gov)
  • Understanding the scope of RGEN-mediated off-target effects in human and other eukaryotic cells will be critically essential if these nucleases are to be used widely for research and therapeutic applications. (cdc.gov)
  • To begin to define the specificity determinants of RGENs in human cells, we sought to perform a large-scale test in which we assessed the effects of systematically mismatching various positions within multiple gRNA/target DNA interfaces. (cdc.gov)
  • ArrayXpress' general strategy is to study cell cultures by collecting samples at multiple time points, performing RNA-Seq to quantify gene expression, mapping the expression data onto biochemical pathways to see how the cells are responding to the task of making a recombinant protein, and analyzing this data at the pathway level to determine what is limiting the production of the protein. (genengnews.com)
  • Mining of the peer-reviewed literature then led to the hypothesis that excess adenine in the medium might be causing the formation of PurR-hypoxanthine complexes, which sensitize the cells to growth arrest by adenosine and inosine, thus reducing protein yields. (genengnews.com)
  • IL-13R alpha 1 is an alternat accessory protein to the common cytokine receptor gamma chain in non-immune cells [2] [3] . (medchemexpress.com)
  • Since its launch, we have been able to demonstrate how beneficial the OneBio integrated biologics development solution can be to sponsors, saving them time on managing multiple partners, and handoffs between companies," said Karen Flynn, Catalent's Interim President, Division Head for BioModalities (Cell, Gene and Protein Therapies). (manufacturingchemist.com)
  • In comparison to DMEM / Ham's F-12 medium, this product allows for cell cultivation with reduced serum supplementation, without affecting cell proliferation rate or morphology. (nacalai.co.jp)
  • We previously showed that cyclin I does not regulate proliferation, but rather controls survival of podocytes, terminally differentiated epithelial cells that are essential for the structural and functional integrity of kidney glomeruli. (jci.org)
  • Soluble IL-4R (sIL-4R) inhibits IL4-mediated cell proliferation and IL-5 up-regulation by T-cells. (medchemexpress.com)
  • 3 d) inhibits IL-4-mediated proliferation and IL-5 upregulation by T cells [7] . (medchemexpress.com)
  • HEK-293 cells were subjected to SDS PAGE followed by western blot with 15287-1-AP (HSPB8 antibody) at dilution of 1:500 incubated at room temperature for 1.5 hours. (ptglab.com)
  • Catalent has expanded its integrated development, manufacturing and supply solution, OneBio Suite, across a range of biologic modalities, including antibody and recombinant proteins, cell and gene therapies, and mRNA. (manufacturingchemist.com)
  • It has been demonstrated that α-syn can be secreted from neuronal cells, enter other neighboring cells, and seed small intracellular aggregates [ 31 ]. (aging-us.com)
  • After presumably adapting to tissue culture, cells from this clone developed into the relatively stable HEK 293 line. (wikipedia.org)
  • However, the original adenovirus transformation was inefficient, suggesting that the cell that finally produced the HEK 293 line may have been unusual in some fashion. (wikipedia.org)
  • An embryonic adrenal precursor cell therefore seems the most likely origin cell of the HEK 293 line. (wikipedia.org)
  • The first reference to the cell line as "293T" may be its use to create the BOSC23 packaging cell line for producing retroviral particles. (wikipedia.org)
  • Interleukin-4R alpha (IL-4Rα), also known as CD124 and B cell stimulatory factor (BSF) receptor, is one of the anti-inflammatory cytokines, and highly expressed in activated T-cells [1] . (medchemexpress.com)
  • Flow Cyt (intra): NIH/3T3 and HeLa cells. (abcam.com)
  • To address this an ubiquitination assay was performed in HeLa cells expressing HA-tagged ubiquitin in which lysine 48 or 63 was mutated to arginine (HA-Ub WT HA-Ub K48R and HA-Ub K63R). (bioskinrevive.com)
  • Interestingly the conversation between endogenous MULAN and Akt was detected in the presence of serum and insulin in HeLa cells (Physique 3A). (bioskinrevive.com)
  • We stably engineered O-glycan sulfation capacities in HEK293 cells by site-directed knockin of sulfotransferase genes in combination with knockout of genes to eliminate endogenous O-glycan branching (core2 synthase gene GCNT1) and/or sialylation capacities in order to provide simplified substrates (core1 Galβ1-3GalNAcα1-O-Ser/Thr) for the introduced sulfotransferases. (lu.se)
  • long-term cells for smooth genes. (scoutconnection.com)
  • GFAP is heavily and specifically expressed in astrocytes and certain astroglia of the central nervous system, in satellite cells of peripheral ganglia, and in non-myelinating Schwann cells of peripheral nerves. (thermofisher.com)
  • The 5HT 3 receptor (5HT 3 R) is a serotonin-gated ion channel whose expression is restricted to a subset of cells within the central and peripheral nervous systems. (jneurosci.org)
  • the original HEK 293 cell clone was from his 293rd experiment. (wikipedia.org)
  • precession cell and its lox in a receptor. (scoutconnection.com)
  • For the type I receptor, depends on IL-4R alpha binding IL-4 to recruit IL-2R gamma chain in immune cells. (medchemexpress.com)
  • Expression of the galactose 3-O-sulfotransferase 2 in HEK293 cells resulted in sulfation of core1 and core2 O-glycans, whereas expression of galactose 3-O-sulfotransferase 4 resulted in sulfation of core1 only. (lu.se)
  • P.987 left column 4th paragraph: 'In summary, here [investigators] have developed an imaging method that enables the measurement of ribosome initiation and translocation rates on single mRNA molecules in live cells. (harvard.edu)
  • P.979 right column bottom paragraph: 'Next, [investigators] measured the translocation speed of ribosomes on single mRNAs by treating cells with harringtonine, a small molecule inhibitor of translation that stalls new ribosomes at the start of the mRNA coding sequence without affecting ribosomes further downstream (Ingolia et al. (harvard.edu)
  • Bioreactors with rocker platforms, which literally rock the cell cultures back and forth, were introduced about a decade ago and have since become widely accepted for the development of seed cultures, says Loe Hubbard, applications manager of Pall's cell culture systems. (genengnews.com)
  • U2OS.EGFP cells caused by inactivating frameshift insertion/deletion (indel) mutations introduced by error prone non-homologous end-joining (NHEJ) repair of nuclease-induced double-stranded breaks (DSBs) (Fig. 1a and Methods ). (cdc.gov)
  • Antibodies to GFAP are very useful as markers of astrocytic cells. (thermofisher.com)
  • First, we determined the endotoxin content of all the materials, a prerequisite for any studies using immune-competent cells. (cdc.gov)
  • For many years it was assumed that HEK 293 cells were generated by transformation of either a fibroblastic, endothelial or epithelial cell, all of which are abundant in kidneys. (wikipedia.org)
  • Cyclin I is an atypical cyclin because it is most abundant in postmitotic cells. (jci.org)
  • We chose to define promoter elements within the 5HT 3 R gene because it is prominently expressed in a subset of sensory neurons, as well as in neuroblastoma cell lines, thereby facilitating promoter analysis in vitro . (jneurosci.org)
  • Using THP-1 knockdown cell lines, we found that IL-1beta secretion was caspase-1-, ASC-, and NLRP3- dependent. (cdc.gov)
  • As a consequence, HEK 293 cells should not be used as an in vitro model of typical kidney cells. (wikipedia.org)
  • HEK 293 and CHO cells were cultured using both this product and Company A's serum-reduced medium. (nacalai.co.jp)
  • Moreover LY294002 a PI3K inhibitor that inhibits the phosphorylation of Akt suppressed MULAN-induced Akt ubiquitination in serum-stimulated HEK293 cells (Physique 3C lanes 5-8). (bioskinrevive.com)
  • We used the engineered cell library to dissect the binding specificity of galectin-4 and confirmed binding to the 3-O-sulfo-core1 O-glycan. (lu.se)
  • IL-4 R alpha soluble isoform 1 can be produced by proteolytic cleavage at the cell surface (shedding) by a metalloproteinase [4] . (medchemexpress.com)
  • Besides their toxic properties in cell culture experiments [ 12 ], α-syn oligomers are able to induce Parkinson-like symptoms in animal models [ 13 ]. (aging-us.com)
  • In addition, neural stem cells strongly express GFAP. (thermofisher.com)
  • In addition, "We see less cell debris at the end of the run," she says. (genengnews.com)
  • The cells were obtained from a single, aborted or miscarried fetus, the precise origin of which is unclear. (wikipedia.org)
  • The current through hERG channel was measured by changing the membrane voltage before and after treatment with 31 herbal formulae in HEK 293 cell overexpressing hERG channel using a whole-cell patch clamp system. (jkom.org)
  • IP: K562 whole cell lysate. (abcam.com)
  • GFAP is also found in the lens epithelium, Kupffer cells of the liver, in some cells in salivary tumors and has been reported in erythrocytes. (thermofisher.com)
  • IL-4R alpha participates in forming two interleukin receptors in different cell types. (medchemexpress.com)
  • The HEK 293 pattern most closely resembled that of adrenal cells, which have many neuronal properties. (wikipedia.org)
  • Their efforts can be thwarted by problems ranging from incomplete control over cells' growth conditions to inadequate post-translational modifications. (genengnews.com)
  • GFAP is used as a marker to distinguish astrocytes from other glial cells during development. (thermofisher.com)
  • Emerging evidence suggests that α-syn oligomers spread from cell-to-cell and encourage the propagation of neurodegeneration in a prion-like manner [ 26 ]. (aging-us.com)