Incorporation of biotinyl groups into molecules.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.
An enzyme which catalyzes the release of BIOTIN from biocytin. In human, defects in the enzyme are the cause of the organic acidemia MULTIPLE CARBOXYLASE DEFICIENCY or BIOTINIDASE DEFICIENCY.
A 60-kDa extracellular protein of Streptomyces avidinii with four high-affinity biotin binding sites. Unlike AVIDIN, streptavidin has a near neutral isoelectric point and is free of carbohydrate side chains.
A specific protein in egg albumin that interacts with BIOTIN to render it unavailable to mammals, thereby producing biotin deficiency.
The form of fatty acid synthase complex found in BACTERIA; FUNGI; and PLANTS. Catalytic steps are like the animal form but the protein structure is different with dissociated enzymes encoded by separate genes. It is a target of some ANTI-INFECTIVE AGENTS which result in disruption of the CELL MEMBRANE and CELL WALL.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
The neonatal form of MULTIPLE CARBOXYLASE DEFICIENCY that is caused by a defect or deficiency in holocarboxylase synthetase. HLCS is the enzyme that covalently links biotin to the biotin dependent carboxylases (propionyl-CoA-carboxylase, pyruvate carboxylase, and beta-methylcrotonyl-CoA carboxylase).
Narrowing or constriction of a coronary artery.
Established cell cultures that have the potential to propagate indefinitely.
A group of enzymes that catalyze the transfer of carboxyl- or carbamoyl- groups. EC 2.1.3.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.
A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA (From Enzyme Nomenclature, 1992) EC 6.4.1.2.
The turning off of GENETIC TRANSCRIPTION in certain regions of CHROMATIN without changes in the DNA sequence. Typically epigenetic repression is a way that developmental changes are programmed at the cellular level.
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.
A deficiency in the activities of biotin-dependent enzymes (propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, and PYRUVATE CARBOXYLASE) due to one of two defects in BIOTIN metabolism. The neonatal form is due to HOLOCARBOXYLASE SYNTHETASE DEFICIENCY. The late-onset form is due to BIOTINIDASE DEFICIENCY.
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.
A cytosolic carbonic anhydrase isoenzyme primarily expressed in ERYTHROCYTES, vascular endothelial cells, and the gastrointestinal mucosa. EC 4.2.1.-
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
An essential amino acid. It is often added to animal feed.
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.
Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.
Dental care for patients with chronic diseases. These diseases include chronic cardiovascular, endocrinologic, hematologic, immunologic, neoplastic, and renal diseases. The concept does not include dental care for the mentally or physically disabled which is DENTAL CARE FOR DISABLED.
A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.
Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.
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.
Proteins obtained from ESCHERICHIA COLI.
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.
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 cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.
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.
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.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
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 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.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
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 domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)
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 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.
The marking of biological material with a dye or other reagent for the purpose of identifying and quantitating components of tissues, cells or their extracts.
Anaerobic hyperthermophilic species of ARCHAEA, isolated from hydrothermal fluid samples. It is obligately heterotrophic with coccoid cells that require TRYPTOPHAN for growth.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
A family of plasma membrane neurotransmitter transporter proteins that couple the uptake of GLUTAMATE with the import of SODIUM ions and PROTONS and the export of POTASSIUM ions. In the CENTRAL NERVOUS SYSTEM they regulate neurotransmission through synaptic reuptake of the excitatory neurotransmitter glutamate. Outside the central nervous system they function as signal mediators and regulators of glutamate metabolism.
Straight tubes commencing in the radiate part of the kidney cortex where they receive the curved ends of the distal convoluted tubules. In the medulla the collecting tubules of each pyramid converge to join a central tube (duct of Bellini) which opens on the summit of the papilla.
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.
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
Transport proteins that carry specific substances in the blood or across cell membranes.
Na-K-Cl transporter in the ASCENDING LIMB OF LOOP OF HENLE. It mediates active reabsorption of sodium chloride and is inhibited by LOOP DIURETICS such as FUROSEMIDE; and BUMETANIDE. Mutations in the gene encoding SLC12A1 are associated with a BARTTER SYNDROME.
Sodium channels found on salt-reabsorbing EPITHELIAL CELLS that line the distal NEPHRON; the distal COLON; SALIVARY DUCTS; SWEAT GLANDS; and the LUNG. They are AMILORIDE-sensitive and play a critical role in the control of sodium balance, BLOOD VOLUME, and BLOOD PRESSURE.
A genus of gram-positive, rod-shaped bacteria whose cells occur singly, in pairs or short chains, in V or Y configurations, or in clumps resembling letters of the Chinese alphabet. Its organisms are found in cheese and dairy products as well as on human skin and can occasionally cause soft tissue infections.
A genus of microaerophilic, gram-negative bacteria that forms crystals of the mineral magnetite in special organelles called MAGNETOSOMES.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
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.
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 parts of a macromolecule that directly participate in its specific combination with another molecule.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A chloride channel that regulates secretion in many exocrine tissues. Abnormalities in the CFTR gene have been shown to cause cystic fibrosis. (Hum Genet 1994;93(4):364-8)
Proteins prepared by recombinant DNA technology.
New World marsupials of the family Didelphidae. Opossums are omnivorous, largely nocturnal and arboreal MAMMALS, grow to about three feet in length, including the scaly prehensile tail, and have an abdominal pouch in which the young are carried at birth.
Sodium chloride-dependent neurotransmitter symporters located primarily on the PLASMA MEMBRANE of dopaminergic neurons. They remove DOPAMINE from the EXTRACELLULAR SPACE by high affinity reuptake into PRESYNAPTIC TERMINALS and are the target of DOPAMINE UPTAKE INHIBITORS.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Human colonic ADENOCARCINOMA cells that are able to express differentiation features characteristic of mature intestinal cells, such as ENTEROCYTES. These cells are valuable in vitro tools for studies related to intestinal cell function and differentiation.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Proteins found in any species of bacterium.

A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. (1/1806)

The nature of the broad substrate specificity phenomenon, as manifested by multidrug resistance proteins, is not yet understood. In the Escherichia coli multidrug transporter, MdfA, the hydrophobicity profile and PhoA fusion analysis have so far identified only one membrane-embedded charged amino acid residue (E26). In order to determine whether this negatively charged residue may play a role in multidrug recognition, we evaluated the expression and function of MdfA constructs mutated at this position. Replacing E26 with the positively charged residue lysine abolished the multidrug resistance activity against positively charged drugs, but retained chloramphenicol efflux and resistance. In contrast, when the negative charge was preserved in a mutant with aspartate instead of E26, chloramphenicol recognition and transport were drastically inhibited; however, the mutant exhibited almost wild-type multidrug resistance activity against lipophilic cations. These results suggest that although the negative charge at position 26 is not essential for active transport, it dictates the multidrug resistance character of MdfA. We show that such a negative charge is also found in other drug resistance transporters, and its possible significance regarding multidrug resistance is discussed.  (+info)

Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. (2/1806)

The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle, this protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of post-translational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the post-translational attachment of biotin to a single lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit of acetyl-CoA carboxylase, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxy-biotinylated form of BCCP interacts with transcarboxylase in the transfer of the carboxylate to acetyl-CoA to form malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. The NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment (residue 70-156) of BCCP (holoBCCP87) and the crystal structure of the biotinylated form of a C-terminal fragment (residue 77-156) of BCCP from Escherichia coli acetyl-CoA carboxylase have previously been determined. Comparative analysis of these structures provided evidence for small, localized conformational changes in the biotin-binding region upon biotinylation of the protein. These structural changes may be important for regulating specific protein-protein interactions. Since the dynamic properties of proteins are correlated with local structural environments, we have determined the relaxation parameters of the backbone 15N nuclear spins of holoBCCP87, and compared these with the data obtained for the apo protein. The results indicate that upon biotinylation, the inherent mobility of the biotin-binding region and the protruding thumb, with which the biotin group interacts in the holo protein, are significantly reduced.  (+info)

Streptavidin facilitates internalization and pulmonary targeting of an anti-endothelial cell antibody (platelet-endothelial cell adhesion molecule 1): a strategy for vascular immunotargeting of drugs. (3/1806)

Conjugation of drugs with antibodies to surface endothelial antigens is a potential strategy for drug delivery to endothelium. We studied antibodies to platelet-endothelial adhesion molecule 1 (PECAM-1, a stably expressed endothelial antigen) as carriers for vascular immunotargeting. Although 125I-labeled anti-PECAM bound to endothelial cells in culture, the antibody was poorly internalized by the cells and accumulated poorly after intravenous administration in mice and rats. However, conjugation of biotinylated anti-PECAM (b-anti-PECAM) with streptavidin (SA) markedly stimulated uptake and internalization of anti-PECAM by endothelial cells and by cells expressing PECAM. In addition, conjugation with streptavidin markedly stimulated uptake of 125I-labeled b-anti-PECAM in perfused rat lungs and in the lungs of intact animals after either intravenous or intraarterial injection. The antioxidant enzyme catalase conjugated with b-anti-PECAM/SA bound to endothelial cells in culture, entered the cells, escaped intracellular degradation, and protected the cells against H2O2-induced injury. Anti-PECAM/SA/125I-catalase accumulated in the lungs after intravenous injection or in the perfused rat lungs and protected these lungs against H2O2-induced injury. Thus, modification of a poor carrier antibody with biotin and SA provides an approach for facilitation of antibody-mediated drug targeting. Anti-PECAM/SA is a promising candidate for vascular immunotargeting of bioactive drugs.  (+info)

Molecular biology of biotin attachment to proteins. (4/1806)

Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins.  (+info)

Human biotinidase isn't just for recycling biotin. (5/1806)

For years, the major role of biotin has been as the coenzyme for four carboxylases in humans. Although there has been evidence that biotin might have other functions, none has been firmly established. The discovery that human serum biotinidase has biotinyl-transferase activity, in addition to biotinidase hydrolase activity, presents new possibilities for the role of biotinidase in biotin metabolism. Specific transfer of biotin to histones by biotinidase provides a possible explanation for why biotin is found in the nucleus and the nature of its role in the regulation of protein transcription. Future studies will help to determine the functions of biotinidase in biotin metabolism and in disease states.  (+info)

Treatment of mouse oocytes with PI-PLC releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) protein clusters from the egg surface and inhibits sperm-oolemma binding and fusion. (6/1806)

The effect of phosphatidyinositol-specific phospholipase C (PI-PLC) on mouse sperm-egg interaction was investigated in this study to determine if glycosyl-phosphatidylinositol (GPI)-anchored proteins are involved in mammalian fertilization. When both sperm and zona-intact oocytes were pretreated with a highly purified preparation of PI-PLC and coincubated, there was no significant effect on sperm-zona pellucida binding; however, fertilization was reduced from 59.6% (control group) to 2.8% (treatment group). A similar reduction in fertilization rates was found when zona-intact oocytes were treated with PI-PLC and washed prior to incubation with untreated sperm. The effect of PI-PLC on sperm binding and fusion with zona-free oocytes was then investigated. Treatment of sperm with PI-PLC had no significant effect on sperm-egg binding or fusion. However, treatment of eggs with PI-PLC significantly reduced sperm-egg binding and fusion from 6.2 bound and 2.1 fused sperm per egg in the control group to 2.1 bound and 0.02 fused sperm per egg in the treatment group. This decrease in sperm-egg binding and fusion depended on the dose of PI-PLC employed, with a maximal inhibitory effect on binding and fusion at 5 and 1 U/ml, respectively. PI-PLC-treated oocytes could be artificially activated by calcium ionophore, demonstrating that the oocytes were functionally viable following treatment. Furthermore, treatment of oocytes with PI-PLC did not reduce the immunoreactivity of the non-GPI-anchored egg surface integrin, alpha6beta1. Taken together, these observations support the hypothesis that PI-PLC affects fertilization by specifically releasing GPI-anchored proteins from the oolemma. In order to identify the oolemmal GPI-anchored proteins involved in fertilization, egg surface proteins were labeled with sulfo-NHS biotin, treated with PI-PLC, and analyzed by two-dimensional gel electrophoresis followed by avidin blotting. A prominent high-molecular-weight protein cluster (approximately 70 kDa, pI 5) and a lower molecular weight (approximately 35-45 kDa, pI 5.5) protein cluster were released from the oolemmal surface as a result of PI-PLC treatment. It is likely that these GPI-anchored egg surface proteins are required for sperm-egg binding and fusion.  (+info)

Critical relationship between glycosylation of recombinant lutropin receptor ectodomain and its secretion from baculovirus-infected insect cells. (7/1806)

The lutropin receptor ectodomain overexpressed under the control of the powerful polyhedrin promoter in baculovirus-infected Sf9 insect cells, is mainly found in an inactive, intracellularly-aggregated form. It is secreted in an active form under the control of the P10 promoter, a somewhat weaker and earlier promoter, at the price of a lower production. The apparent molecular masses of the two species encoded by the same cDNA are 48 kDa and 60-68 kDa, respectively. The relationship between the extent and type of glycosylation and the extracellular targeting for the recombinant lutropin receptor ectodomains was investigated precisely with endoglycosidases, lectins of various specificities, and a glycosylation inhibitor, and tested with monoclonal and polyclonal antibodies. The results indicate that the strong polyhedrin promoter probably overwhelms the processing capacity of the ER in Sf9 cells, so that only a high-mannose precursor is expressed in large amounts. Only a minute amount of protein is secreted, which has been processed by Sf9 exoglycosidases/glycosyltransferases and bears complex/hybrid oligosaccharides. The weaker P10 promoter allows secretion of a mature and active receptor ectodomain, bearing complex glycosylation. An important O-linked glycosylation is also added post-translationally on this species. In particular, beta-galactose and sialic acid residues were specifically detected in the secreted species, evidence of the induction of the corresponding glycosyltransferases or of their genes. These results suggest that Sf9 cells should eventually be engineered with chaperones and glycosyltransferases in order to improve the production of demanding glycoproteins such as the porcine lutropin ectodomain, so as to open the way to resolution of the three-dimensional structures of these receptors.  (+info)

Characterization of the internalization pathways for the cystic fibrosis transmembrane conductance regulator. (8/1806)

Mutations in the gene encoding the cystic fibrosis (CF) transmembrane conductance regulator (CFTR) chloride channel give rise to the most common lethal genetic disease of Caucasian populations, CF. Although the function of CFTR is primarily related to the regulation of apical membrane chloride permeability, biochemical, immunocytochemical, and functional studies indicate that CFTR is also present in endosomal and trans Golgi compartments. The molecular pathways by which CFTR is internalized into intracellular compartments are not fully understood. To define the pathways for CFTR internalization, we investigated the association of CFTR with two specialized domains of the plasma membrane, clathrin-coated pits and caveolae. Internalization of CFTR was monitored after cell surface biotinylation and quantitation of cell surface CFTR levels after elution of cell lysates from a monomeric avidin column. Cell surface levels of CFTR were determined after disruption of caveolae or clathrin-coated vesicle formation. Biochemical assays revealed that disrupting the formation of clathrin-coated vesicles inhibited the internalization of CFTR from the plasma membrane, resulting in a threefold increase in the steady-state levels of cell surface CFTR. In contrast, the levels of cell surface CFTR after disruption of caveolae were not different from those in control cells. In addition, although our studies show the presence of caveolin at the apical membrane domain of human airway epithelial cells, we were unable to detect CFTR in purified caveolae. These results suggest that CFTR is constitutively internalized from the apical plasma membrane via clathrin-coated pits and that CFTR is excluded from caveolae.  (+info)

Target carboxyl groups for biotin labeling using amine-derivatized biotin molecules. Choose the best carboxyl biotinylation reagents for your application!
Biotinylation reagents enable isolation, separation, concentration and further downstream processing or analysis of biomolecules.
This unit describes a system for expression of biotinylated proteins in mammalian cells in vivo, and its application to chromatin immunoprecipitation (ChIP)
R&D Systems has an exclusive range of biotinylated recombinant proteins tested for bioactivity to ensure specificity. Asses protein interactions in a range of assay formats, including immunoprecipitation, flow cytometry, immunoassays and surface plasmon resonance.
BirA can be easily found in E. coli. So you can get the gene with following 1st primer. Also our kit can synthesize it as In vitro ...
Human VEGF protein (BT293) is manufactured by R&D Systems, over 95% purity. Reproducible results in bioactivity assays. Learn More...
The One-Step Antibody Biotinylation Kit is optimized for the rapid and simple biotinylation of antibodies. The lyophilized labeling agent allows the simple resuspension and incubation with the antibody of choice, after which the biotinylated antibody can be directly used. - Österreich
Since its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications
Since its discovery in the first half of the twentieth century, the high‐affinity, noncovalent interaction between biotin (vitamin H) and the avian protein avidin (and its bacterial homologs) has been exploited for many diverse biotechnology applications
Project SummaryDuring embryogenesis or wound healing, neighboring cells maintain contact and migrate collectively, thoughthe roles of cell-cell adhesion during collective cell migration is poorly defined. Due to constant pulling andpushing between migrating neighboring cells, we hypothesize that mechanical forces regulate theinteraction between the cell-cell adhesion complex and the actin cytoskeleton, and therefore, theadhesive strength. To identify force-sensitive protein complexes at cell-cell junctions, our innovativebiochemical analysis combines in situ proximal biotin labeling with a cell stretch device that promotes theformation of force-sensitive complexes. By fusing ?-catenin with a promiscuous biotin ligase, any proximalproteins of ?-catenin will be biotinylated. The force-dependent change in the biotinylation profile is an indicationof altered protein complexes. Our preliminary study demonstrates that ?-catenin and myosin IIA are likelyinteracting in a force-dependent manner. While ...
Surface biotinylation and NeutrAvidin pull-down were performed similar to what has been described previously (Zha et al., 2009a; Jing et al., 2011). For biotinylation of organotypic hippocampal slices, each filter, which contained 6-8 slices, was cut out and put in a six-well plate. CHO cells or slices were then washed three times with ice-cold PBS+/+, followed by 30 min incubation at 4°C in 1.5 ml (for CHO cells in 60 mm dishes) or 1 ml (for slices in each well of the 6-well plate) of PBS+/+ containing 0.5 mg/ml Sulfo-NHS-LC-Biotin. Cells were washed once with cold PBS+/+ and the reaction was quenched by 100 mm glycine in PBS+/+. Of note, it is essential, especially for biotinylation of slices, to keep the solution and plates ice cold during the whole procedure. Cells were lysed in 300 μl of NeutrAvidin lysis buffer (PBS, 1% Triton, 0.5% SDS, 0.5 mg/ml N-ethylmaleimide, with protease inhibiters). Cell lysates were sonicated briefly and centrifuged at full speed with a desktop centrifuge for ...
Biotinylated histone H2A peptide acetylated methylated phosphorylated for use in enzyme assays, histone binding and pulldown experiments
Biotinylated histone H3 peptide acetylated methylated phosphorylated for use in enzyme assays, histone binding and pulldown experiments
Product Information Request - SuperSignal West Pico COMPLETE Biotinylated Protein Detection Kit from Pierce Biotechnology, Inc.,,biological,biology supply,biology supplies,biology product
Abstract: Abstract Background Glioblastoma multiformae (GBM) is the most aggressive type of malignant brain tumor with complex molecular profile. Overexpression of Na+/H+ Exchanger isoform 9 (NHE9) promotes tumor progression and correlates positively with insensitivity to radiochemotherapy and poor prognosis. However, molecular mechanisms responsible for increase in NHE9 levels beyond a critical threshold have not been identified. Methods Bioinformatics analysis, luciferase reporter assays, real-time PCR and western blotting were conducted to examine the expression profiles and identify microRNAs (miRNA) that target NHE9. Cell proliferation and migration assays were conducted in U87 glioblastoma cells to determine the consequence of miRNA mediated targeting of NHE9. Endosomal pH measurements, immunofluorescence microscopy and surface biotinylation experiments were conducted to characterize the mechanistic basis of regulation. Results We show that microRNA 135a (miR-135a) targets NHE9 to ...
We performed bio-ChIP-seq using streptavidin beads immunoprecipitation of biotinylated 5 cardiac transcription factors (fbio) and P300 antibody ChIP-seq. We used a dox-inducible dual adenovirus system to express biotinylated Core Cardiac TFs in HL1. One adenovirus expressed the dox-activated reverse tet activator protein (rtTA) and the E. coli biotinylating enzyme BirA from the cardiac specific rat troponin T promoter. The second virus expressed a Core Cardiac TF fused to a C-terminal flag-bio epitope tag, where bio is the 15 amino acid substrate for BirA. This in vivo biotinylation approach permits pulldown of different factors to be performed under identical, stringent conditions, and circumvents limitations posed by available antibodies. We titrated adenovirus and dox doses to express GATA4flbio and MEF2Aflbio at near endogenous levels. The same conditions were then used to express SRFflbio, TBX5flbio, and NKX2-5flbio. Reference: 12. de Boer E, Rodriguez P, Bonte E, Krijgsveld J, Katsantoni E ...
Sulfo-NHS-Biotin is a water soluble biotinylation reagent. Sulfo-NHS-Biotin is ideal for biotinylating antibody or protein that can then be used for protein detection or immobilization.
TY - JOUR. T1 - Signature Fragment Ions of Biotinylated Peptides. AU - Renuse, Santosh. AU - Madugundu, Anil K.. AU - Jung, Jae Hun. AU - Byeon, Seul Kee. AU - Goldschmidt, Hana L.. AU - Tahir, Raiha. AU - Meyers, David. AU - Kim, Dae In. AU - Cutler, Jevon. AU - Kim, Kwang Pyo. AU - Wu, Xinyan. AU - Huganir, Richard L.. AU - Pandey, Akhilesh. PY - 2020/2/5. Y1 - 2020/2/5. N2 - The use of biotin or biotin-containing reagents is an essential component of many protein purification and labeling technologies. Owing to its small size and high affinity to the avidin family of proteins, biotin is a versatile molecular handle that permits both enrichment and purity that is not easily achieved by other reagents. Traditionally, the use of biotinylation to enrich for proteins has not required the detection of the site of biotinylation. However, newer technologies for discovery of protein-protein interactions, such as APEX and BioID, as well as some of the click chemistry-based labeling approaches have ...
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TY - JOUR. T1 - CCL2 promotes P2X4 receptor trafficking to the cell surface of microglia. AU - Toyomitsu, Emika. AU - Tsuda, Makoto. AU - Yamashita, Tomohiro. AU - Tozaki-Saitoh, Hidetoshi. AU - Tanaka, Yoshitaka. AU - Inoue, Kazuhide. PY - 2012/6/1. Y1 - 2012/6/1. N2 - P2X4 receptors (P2X4Rs), a subtype of the purinergic P2X family, play important roles in regulating neuronal and glial functions in the nervous system. We have previously shown that the expression of P2X4Rs is upregulated in activated microglia after peripheral nerve injury and that activation of the receptors by extracellular ATP is crucial for maintaining nerve injury-induced pain hypersensitivity. However, the regulation of P2X4R expression on the cell surface of microglia is poorly understood. Here, we identify the CC chemokine receptor CCR2 as a regulator of P2X4R trafficking to the cell surface of microglia. In a quantitative cell surface biotinylation assay, we found that applying CCL2 or CCL12, endogenous ligands for ...
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A gray area at times. Have used the Scytek kit (check out website) for frozen sections, but did not use their peroxidase blocker, it ate frozens off the slide. Substituted a Dako peroxidase blocker for frozens was much friendlier. The kicker with this kit, their special blocker is excellent, and you have to use their chromogen with this kit. What really worked for us was to use their two blockers (not the peroxidase block though),a biotinylated primary in place of a secondary antibody with the Scytek kit since we did not have a purified primary on hand. We also diluted out the biotinylated primary further, so do a more extended dilution panel, this reduced our cross reaction background. This is the basis of the DAKO ARK kit, biotinylating the primary, some antibodies don biotinylate as well, a potential problem, but may work with yours, so another option - DAKO ARK kit. There are others on the market, Zymed, Innovex, Vector MOM kit, etc, all worth a try. Have heard some mixed reviews on Mouse ...
I wish to immobilise a peptide on a column. I think the easiest way to do this would be to biotinylate the peptide at the C-terminus and link it to streptavidin-agarose. a) Is this true? b) What is the easiest way to biotinylate specifically on the C-terminus of a peptide - do I link through a cysteine? c) How do I get rid of free biotin from a small peptide (approx. 2kD ...
Non-Radioactive Translation Detection Systems for colorimetric detection of proteins synthesized in vitro. Biotinylated proteins are detected using Streptavidin-Alkaline Phosphatase or Streptavidin-HRP.
Just for the sake of completing this thread, Ive decided to do a cell surface receptor biotinylation assay. Basically, incubating cells with biotin (in cold PBS) which binds to all available primary amines on the cell surface. After 1h of incubation, un-bound biotin will be inactivated by incubating the cells in 50mM Tris pH 8 for 5 min. After that, I will lyse the cells and precipitate surface proteins with streptavidin agarose. Finally, the cells surface receptor will be visualized through western blotting.. ...
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Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
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Whatever the assay you have in mind, you need the right technologies for your target. We can custom conjugate your antibody or biomolecule to any bead, or biotinylate or DIG-label your targets, so you can develop the assay you need. If you prefer, we can even perform the assay development for you.
TY - JOUR. T1 - Ultrasensitive immuno-detection using viral nanoparticles with modular assembly using genetically-directed biotinylation. AU - Litvinov, Julia. AU - Hagström, Anna E V. AU - Lopez, Yubitza. AU - Adhikari, Meenu. AU - Kourentzi, Katerina. AU - Strych, Ulrich. AU - Monzon, Federico A.. AU - Foster, William. AU - Cagle, Philip T.. AU - Willson, Richard C.. PY - 2014. Y1 - 2014. N2 - We report a novel, modular approach to immuno-detection based on antibody recognition and PCR read-out that employs antibody-conjugated bacteriophage and easily-manipulated non-pathogenic viruses as affinity agents. Our platform employs phage genetically tagged for in vivo biotinylation during phage maturation that can easily be linked, through avidin, to any biotinylated affinity agent, including full-length antibodies, peptides, lectins or aptamers. The presence of analyte is reported with high sensitivity through real-time PCR. This approach avoids the need to clone antibody-encoding DNA fragments, ...
Regulation of the expression of the gene(s) coding for the 78-kD, biotin-containing subunit of [beta]-methylcrotonyl-coenzyme A carboxylase (MCCase) was investigated in different organs of tomato (Lycopersicon esculantus) plants. The specific activity of MCCase is highest in extracts from roots, followed in descending order by ripe and ripening fruits, stems, and leaves. The specific activity is 10-fold higher in roots than in leaves. However, the steady-state levels of the 78-kD subunit of MCCase and its mRNA are approximately equal in both roots and leaves. Instead, the difference in MCCase activity between these two organs is directly correlated to the biotinylation status of the enzymes biotin-containing subunit. Thus, the lower activity of MCCase in leaves is attributed to the reduced biotinylation of the biotin-containing subunit of the enzyme. Consistent with this model, a pool of nonbiotinylated enzyme is present in leaves, whereas the nonbiotinylated enzyme is undetectable in roots. ...
The attachment of biotin to various chemical sites, called biotinylation, can be used as an important laboratory technique to study various processes including DNA transcription and replication. Biotin itself is known to biotinylate histones, but is not found naturally on DNA.. Biotin binds very tightly to the tetrameric protein streptavidin, with a dissociation constant Kd in the order of 10-15 mol/L (Bonjour 1977, Green 1975) or 4x10-14 (Holmberg et al. 2005). Holmberg et al. (2005) note that the biotin-streptavidin system is the strongest noncovalent biological interaction known. This is often used in different biotechnological applications. Holmberg et al. showed how to utilize high temperatures to efficiently break the interaction without denaturation of the streptavidin.. In the biology laboratory, biotin is sometimes chemically linked, or tagged, to a molecule or protein for biochemical assays. The specificity of the biotin-streptavidin linkage allow use in molecular, immunological, and ...
If you want to get the best signal to background ratio you should go for biotinylation of your protein so you can do stringent washes. Tagging your protein with biotin ligase recognition peptide and coepressing with biotin ligase will result in the biotinylation of your protein. You can get a very good signal to background ratio this way ...
MHC multimers are oligomeric forms of MHC molecules, designed to identify and isolate T-cells with high affinity to specific antigens amid a large group of unrelated T-cells. Multimers generally range in size from dimers to octamers; however, some companies use even higher quantities of MHC per multimer. Multimers may be used to display class 1 MHC, class 2 MHC, or nonclassical molecules (e.g. CD1d) from species such as monkeys, mice, and humans. Since T-cell receptors have a low affinity for their MHC counterparts, it was historically problematic to label T cells effectively using single MHC-T-cell interactions. However, in 1996 it was proposed by John Altman to use a complex of multiple MHC molecules to form a more stable bond between corresponding T-cells. The most commonly used MHC multimers are tetramers. These are typically produced by biotinylating soluble MHC monomers, which are typically produced recombinantly in eukaryotic or bacterial cells. These monomers then bind to a backbone, ...
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Human HER2 /ErbB2 /CD340 Protein, Biotinylated (Biotinylated rhHER2) Thr 23 - Thr 652 (AAA75493), was labeled with biotin based on rh HER2 Protein, which was produced in human 293 cells (HEK293).
Biotin protein ligase of is the 35. or that the presence of the reaction intermediate impedes access of subtilisin to the cleavage site. The disordered loop containing residues 115C123 lies close to the biotin binding site, and residues 115C118 become ordered in the crystal structure when biotinyl-lysine occupies the active site. Because of the similarity to nucleotide-binding sequences in protein buy 118876-58-7 kinases, the sequence 115GRGRRG120 within this loop had been thought to function in ATP binding (Buoncristiani et al. 1986; Wilson et al. 1992). However, a recent mutational analysis shows that this sequence has a role in biotin binding (Kwon and Beckett 2000). No function has been identified previously for the C-terminal domain comprising residues 274C321, which shows structural similarity to the Src homology 3 domains (Noble et al. 1993). However, recent evidence of safety by biotinyl-5-AMP buy 118876-58-7 against hydroxyl radical cleavage from the BirA backbone at a number of sites ...
Adenoviral vectors have great potential for use in gene therapy and genetic immunization. The targeting of Ad vectors to the relevant tissue and cell types in vivo could greatly improve their safety and performance by lowering the effective dosage required for therapeutic levels of gene expression. Redirection of Ad vector tropism will require physical modifications of the adenoviral capsid but direct genetic modification of the Ad capsid has so far been limited to small peptides. A novel system for the attachment of targeting ligands to the Ad capsid, based on the extremely strong avidin-biotin interaction, is described herein. The genetic insertion of a biotin acceptor peptide (BAP) into the fiber, protein IX, or hexon components of the Ad capsid has resulted in vectors that are metabolically biotinylated upon production in host cells. Avidin-dependent redirection of transduction through a variety of biotinylated ligands is greatly dependent on the nature of the biotinylated capsid protein. ...
In 2012, Roux et al. published a nice paper, that received no less than four article recommendations from F1000 researchers. The paper described a method for tracking the interaction partners a protein has had within a cell (a history of its interacting partners). The method, called BioID, is based on proximity-dependent biotinylation of proteins by a promiscuous biotin ligase mutant BirA (R118G), which is fused to your protein of interest. After an overnight incubation with biotin, cells can be subjected to harsh lysis and biotinylated proteins can be isolated and identified by mass spectroscopy to determine the proteins that had come into contact with the chimeric BirA (R118G) protein. This method is a bit different from standard co-IP or pull-down experiments, because it allows one to identify proteins who interact transiently or weakly with the protein of interest. Also, due to the strong biotin-avidin binding affinity, harsh washes can greatly reduce background protein binding. [Read ...
BirA biotin ligase was expressed as maltose-binding protein (MBP) fusion in an E. coli cells. The dual 6xHis-MBP tag at the N-terminus is useful for removal of BirA after biotinylation through either Ni-NTA or amylose resin columns. Catalog number: MBBL-301 Expression host: Escherichia coli (E. coli). Expressed Region
BirA biotin ligase was expressed as maltose-binding protein (MBP) fusion in an E. coli cells. The dual 6xHis-MBP tag at the N-terminus is useful for removal of BirA after biotinylation through either Ni-NTA or amylose resin columns. Catalog number: MBBL-301 Expression host: Escherichia coli (E. coli). Expressed Region
Avidin and streptavidin reagents are powerful tools to detect or purify biotinylated proteins, nucleic acids, and other macromolecules.
1A6X: Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
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In biochemistry, biotinylation is the entire process of covalently attaching biotin to a protein, nucleic acid or other molecule. Biotinylation is quick, certain and is not likely to perturb the natural operate from the molecule due to the small dimension of biotin (MW = 244.31 g/mol). Biotin binds to streptavidin and avidin with an especially superior affinity, quick on-price, and higher specificity, and these interactions are exploited in many areas of biotechnology to isolate biotinylated molecules of desire. Biotin-binding to streptavidin and avidin is resistant to extremes of heat, pH and proteolysis, earning capture of biotinylated molecules attainable in numerous types of environments ...
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Page contains details about biotin-polyA-tailed DNA-capped citrate-stabilized gold nanoparticles-coated streptavidin-coated magnetic beads . It has composition images, properties, Characterization methods, synthesis, applications and reference articles : nano.nature.com
Proven, cost-efficient LANCE Ultra reagents can be used to quantitate peptide modifications, detecting specific meythylation and acetylation states. No wash, homogenous LANCE Ultra reagents are HTS friendly - design your own epigenetics screening strategy for greatest efficiency.. Epigenetic enzymatic assays are optimized using a biotinylated histone H3-derived peptide as substrate. The modified peptide is captured by the Eu-labeled antibody (Ab) and ULight-Streptavidin (SA) which bring the Eu donor and ULight acceptor dye molecules into close proximity. Upon irradiation at 320 or 340 nm, the energy from the Eu donor is transferred to the ULight acceptor dye which, in turn, generates light at 665 nm. The intensity of the light emission is proportional to the level of biotinylated substrate modification.. ...
To determine selectivity against αIIbβIIIa, wells of a 96-well Immulon-2 microtiter plate were coated with 10 μg/ml RGD affinity-purified human αIIbβIIIa in 10 mM HEPES, 150 mM NaCl, and 1 mM MgCl2, pH 7.4 (500 ng/well αIIbβIIIa final), and then the pate was incubated overnight at 4°C. The next day, the wells were blocked with 5% BSA in the above-mentioned buffer at room temperature for 2 h. The assay plate was washed five times with modified Tyrodes buffer (150 mM NaCl, 12 mM NaHCO3, 2.6 mM KCl, 2.5 mM HEPES, 1 mM MgCl2, and 1 mg/ml BSA, pH 7.4). Biotinylated fibrinogen was prepared using human fibrinogen according to directions from the biotin-X-NHS biotinylation kit. Fifty microliters of the compound/biotinylated fibrinogen mix was transferred to the assay plate and incubated at room temperature for 2 h. After incubation, the assay plate was washed five times with modified Tyrodes buffer. Reactions were visualized as described above. JNJ-26076713 was tested at half-log doses from ...
4GJV: A dual anchoring strategy for the localization and activation of artificial metalloenzymes based on the biotin-streptavidin technology.
Purified Recombinant Human ITGAV & ITGB6 Protein, His-Avi-tagged, Biotinylated from Creative Biomart. Recombinant Human ITGAV & ITGB6 Protein, His-Avi-tagged, Biotinylated can be used for research.
SE arises from deficits in the efficacy of GABAergic inhibition that include altered GABAAR functional expression and pharmacology; however, the mechanisms underlying these deficits remain to be established (Lowenstein and Alldredge, 1998; Alldredge and Lowenstein, 1999). To address this critical question, we have examined the impact of SE on GABAAR functional expression together with the efficacy of synaptic inhibition in hippocampal slices derived from mice injected with pilocarpine. This animal model exhibits many similarities to patients undergoing SE including the development of pharmacoresistance (Kapur and Coulter, 1995; Coulter, 2001).. As measured using biotinylation, the cell surface stability of the GABAAR α1, 2, 4, β3, and γ2 subunits was significantly reduced in SE compared with controls, whereas those encoding the GABABR R1 and R2 subunits were unaltered. In contrast, the cell surface stability of the α5 and δ subunits was significantly increased. Thus, our results demonstrate ...
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Choose from among purified avidin & streptavidin proteins conjugated with a range of fluorophores for fluorescence detection of biotinylated macromolecules in a range of research applications. Click here for more.
MojoSort™ Streptavidin Nanobeads - Streptavidin Nanobeads can be used for positive or negative selection of targeted cells with biotin-conjugated antibodies.
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"Biotinylation by antibody recognition - A method for proximity labeling". Nature Methods. 15 (2): 127-133. doi:10.1038/nmeth. ... "β-Actin mRNA interactome mapping by proximity biotinylation". Proceedings of the National Academy of Sciences. 116 (26): 12863- ...
The tag is recognized by a repertoire of single-domain antibodies AviTag, a peptide allowing biotinylation by the enzyme BirA ... such as biotinylation by biotin ligase) or chemical modification (such as reaction with FlAsH-EDT2 for fluorescence imaging). ...
... biotinylation MeSH E05.393.525.100 - blotting, northern MeSH E05.393.525.150 - blotting, southern MeSH E05.393.525.225 - ...
biotinylation: covalent attachment of a biotin moiety using a biotinylation reagent, typically for the purpose of labeling a ...
Chapman-Smith A, Cronan JE (1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional ...
Basic Protocol 2: Cell Surface Biotinylation. *Basic Protocol 3: In Vivo Biotinylation of Mice Through Intra‐Cardiac Perfusion ... Biotinylation solution: 1 mg/ml sulfo‐NHS‐LC‐biotin (e.g., Thermo Scientific, cat. no. 21335) in 50 mM PBS (pH 7.4)/10% (w/v) ... Basic Protocol 2: Cell Surface Biotinylation. Materials * Cells growing in 75‐cm2 tissue culture flasks and appropriate growth ... In vivo protein biotinylation and sample preparation for the proteomic identification of organ‐ and disease‐specific antigens ...
Choose the best carboxyl biotinylation reagents for your application! ... Choose the best carboxyl biotinylation reagent for your application Product categories. Product. Product features. Spacer arm ( ... Long, hydrophilic reagent for biotinylation of carboxyls via EDC 53.2. Yes. No No ...
Use of protein biotinylation in vivo for immunoelectron microscopic localization of a specific protein isoform. J. Histochem. ... Efficient biotinylation and single‐step purification of tagged transcription factors in mammalian cells and transgenic mice. ... Use of in vivo biotinylation to study protein‐protein and protein‐DNA interactions in mouse embryonic stem cells. Nat. Protoc. ... Codon optimization of the BirA enzyme gene leads to higher expression and an improved efficiency of biotinylation of target ...
The One-Step Antibody Biotinylation Kit is optimized for the rapid and simple biotinylation of antibodies. The lyophilized ... One-Step Antibody Biotinylation Kit. Product overview. The One-Step Antibody Biotinylation Kit is optimized for the rapid and ... The One-Step Antibody Biotinylation Kit has been developed for the biotinylation of monoclonal antibodies for use in magnetic ... The One-Step Antibody Biotinylation Kit has been developed for the biotinylation of monoclonal antibodies for use in magnetic ...
The force-dependent change in the biotinylation profile is an indicationof altered protein complexes. Our preliminary study ... and the extent of biotinylation. Using the newly designed cell stretcher and massspectrometry analysis, we will determine a ...
... enable isolation, separation, concentration and further downstream processing or analysis of ... Biotinylation Reagent Selection Guide. Crosslinker. Acronym. Spacer Arm. Length. M.W.. Reactivity. Cleavable. By. Membrane. ... Appropriate biotinylation of the target molecule is essential to ensure high binding efficiency to streptavidin or Immobilized ... Biotinylation reagents are widely used to enable the isolation, separation, concentration and further downstream processing or ...
As shown below, biotinylation can be done with using biotin ligase and biotin with a BAP tagged fusion protein. ...
Words related to biotinylation:. = 48 && event.charCode <= 57 value="Num letters..." onfocus="inputFocus(this)" onblur=" ...
... Michael Daws Michael.Daws at ucmp.umu.se Mon Nov 13 10:40:06 EST 1995 *Previous message: NEW COMPUTER ...
Kinase-catalyzed biotinylation for phosphoprotein detection.. Green KD1, Pflum MK.. Author information. 1. Department of ...
... the reactive groups of biotinylation reagents and antibody biotinylation reagents. ... This article discusses biotinylation, including reagent solubility, spacer arm length, cleavability or reversibility, ... Biotinylation quantitation Determining the extent of biotin modification after a biotinylation reaction can aid in optimizing a ... Biotinylation reagent solubility The solubility of a biotinylation reagent greatly influences the ability to label target ...
Biotinylation is a natural, albeit rare, modification of human histones.. Kuroishi T1, Rios-Avila L, Pestinger V, Wijeratne SS ... Biotinylation marks can be detected in bulk extracts from human cells, using streptavidin and anti-biotin as probes ... Recently, a team of investigators failed to detect biotinylated histones and proposed that biotinylation is not a natural ... These studies provide unambiguous evidence that biotinylation is a natural, albeit rare, histone modification. Less than 0.001 ...
AirID is a highly active biotinylation enzyme with low toxicity. By using AirID, comprehensive biotinylation of proteins ... In this research, we have developed a biotinylation enzyme, AirID, using an ancestral enzyme reconstruction algorithm. ... Further improvement of biotinylation enzymes is an important goal for enhancing the convenience of proximity biotinylation in ... A new biotinylation enzyme for analyzing protein-protein interactions. Ehime University. Journal. eLife. Funder. Japan Agency ...
Visit CellSignal.com to view our Biotinylated Peptide materials including Protein Biotinylation & more. CST - Customer ...
High impact information on Biotinylation. *Protease and biotinylation accessibility studies of right side-out and inside-out ... Chemical compound and disease context of Biotinylation. *Sequence requirements for the biotinylation of carboxyl-terminal ... Biotinylation of single cysteine mutants of the glutamate transporter GLT-1 from rat brain reveals its unusual topology. ... Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle. Lorenzon, N.M., ...
Biotinylation. Discussion of all aspects of cellular structure, physiology and communication.. Moderators: Leonid, amiradm, ... one question about biotinylation. After biotinyled with BIOTIN, and then lysated cells in RIPA buffer and then added ...
However, TurboID enabled robust biotinylation in the endoplasmic reticulum lumen compared to BioID. Induction of biotinylation ... However, the conventional labeling period requires 15-18 h for robust biotinylation which may not be ideal for some ... For TurboID we observed signs of protein instability, persistent biotinylation in the absence of exogenous biotin, and an ... However, there is reported concern about inducibility of biotinylation, cellular toxicity, and ligase stability. To further ...
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In vivo protein biotinylation for identification of organ-specific antigens accessible from the vasculature. Nat. Methods 2, ... Roesli, C., Neri, D. & Rybak, J. In vivo protein biotinylation and sample preparation for the proteomic identification of organ ... In vivo protein biotinylation and sample preparation for the proteomic identification of organ- and disease-specific antigens ...
Targeting protein biotinylation enhances tuberculosis chemotherapy. By Divya Tiwari, Sae Woong Park, Maram M. Essawy, Surendra ... Targeting protein biotinylation enhances tuberculosis chemotherapy. By Divya Tiwari, Sae Woong Park, Maram M. Essawy, Surendra ... Targeting protein biotinylation enhances tuberculosis chemotherapy Message Subject. (Your Name) has forwarded a page to you ... Because it took several days before exposure to Bio-AMS affected Mtbs pattern of protein biotinylation, we first grew Mtb with ...
... ,Applications,Example for use of B6096,Products,Related Products,Related Product Category ... A [µL of 10 mM biotinylation solution] x 10-6 [L/µL] x 10 [mmol/L] x 10-3 [mol/mmol]. A = 20 [µL of 10 mM biotinylation ... Calculate : A µL of 10 mM biotinylation solution for biotinylation 2 mg IgG (150,000 M.W.). 2 [mg IgG] x 10-3 [g/mg] x 1/ ... Use of a 10 mM biotinylation solution is recommended. In order to efficiently biotinylate a sample, biotinylation solution ...
Biotinylation of bladder tissue was detected by exposing frozen bladder sections (14 μm thick; intact bladders) to strepavidin ... In vivo biotinylation of urothelial cell-surface proteins-twelve male Sprague-Dawley rats (250-300 gm) were anesthetized with ... in Vivo Biotinylation of Urothelial Cell Surface Proteins. We developed a methodology to identify cell-surface protein ... Figure 1: In vivo biotinylation of urothelium. (a) and (c) saline-treated bladders, (b) and (d) SP-treated bladders. Biotin ...
In Vivo Biotinylation of Urothelial Cell-Surface Proteins. Katherine L. Meyer-Siegler,1,2 Shen-Ling Xia,3 and Pedro L. Vera1,4 ...
Two biotinylation-based methods, designed for determining the cell-surface expression and endocytic rate of proteins expressed ... In a typical biotinylation assay, the cells are first washed thoroughly in 4 °C PBS. This removes any traces of serum proteins ... The biotinylation reagent is then added. Next, the cells are washed again, and then incubated with a quenching buffer ... Using cell-surface biotinylation to assess the plasma membrane expression of AQP4 in astrocytes. Laminin-treated astrocyte ...
Regulation of [beta]-Methylcrotonyl-Coenzyme A Carboxylase Activity by Biotinylation of the Apoenzyme. X. Wang, E. S. Wurtele, ... Thus, the lower activity of MCCase in leaves is attributed to the reduced biotinylation of the biotin-containing subunit of the ... Instead, the difference in MCCase activity between these two organs is directly correlated to the biotinylation status of the ... These observations indicate that the posttranslational biotinylation of the biotin-containing sub-unit of MCCase is an ...
A Correction to the Presentation Titled: "Protein Complexes and Target Genes Identification by in Vivo Biotinylation: The STAT5 ... A Correction to the Presentation Titled: "Protein Complexes and Target Genes Identification by in Vivo Biotinylation: The STAT5 ... A Correction to the Presentation Titled: "Protein Complexes and Target Genes Identification by in Vivo Biotinylation: The STAT5 ... A Correction to the Presentation Titled: "Protein Complexes and Target Genes Identification by in Vivo Biotinylation: The STAT5 ...
ESC Biotinylation Streptavidin Multi-protein complexes Purification Mass spectrometry BirA This is a preview of subscription ... Kim J, Cantor AB, Orkin SH, Wang J (2009) Use of in vivo biotinylation to study protein-protein and protein-DNA interactions in ... One such approach relies on in vivo biotinylation of a protein of interest and subsequent pull-down of its interacting partners ... Faiola F., Saunders A., Dang B., Wang J. (2014) An Improved In Vivo Biotinylation Strategy Combined with FLAG and Antibody ...
Biotinylation by Myc-BirA*-TbMORN1 in vivo. Myc-BirA*-TbMORN1 cells were incubated with excess biotin in the presence or ... The Myc-BirA* biotinylation module was found to be nontoxic and permissive for normal localization of tagged protein (Fig. 1). ... Although promiscuous biotinylation by BirA* was first demonstrated in Escherichia coli, the data here constitute-to our ... Novel Bilobe Components in Trypanosoma brucei Identified Using Proximity-Dependent Biotinylation. Brooke Morriswood, Katharina ...
Biotinylation reagents along with LC linker (amino caproic acid) are a good illustration of dPEG excellent performance in ... Sulfo-NHS-LC-biotin is probably the most popular biotinylation currently available on the market. The hydrophilic LC linker is ...
Trafficking of immature ΔF508-CFTR to the plasma membrane and its detection by biotinylation. Yishan Luo, Ken McDonald, John W. ... Intracellular biotinylation was reduced when cells were treated with sulfo-NHS-LC-biotin (biotin attached to a reactive NHS ... Trafficking of immature ΔF508-CFTR to the plasma membrane and its detection by biotinylation ... Trafficking of immature ΔF508-CFTR to the plasma membrane and its detection by biotinylation ...
Metabolic biotinylation of the adenoviral capsid: Avidin-based applications and studies of ligand-targeted gene delivery. ...
Home > Categories > Chemicals > Antibody Synthesis And Biotinylation Reagents .menu h1{ display: none;} .current_id{ font- ... SO4 group keeps biotinylation localized at the cell, Sulfo-NHS ester group wil ... SO4 keeps biotinylation localized at the cell surface, Eliminates need for har ...
Creative BioLabs has developed a unique protein and antibody site-specific biotinylation BtAP-Tag® platform for antibody and ... Protein and Antibody Biotinylation. Protein and Antibody Biotinylation. "Creative Biolabs is committed to providing highly ... Biotinylation by this platform allows sensitive recognition by avidin or streptavidin that is conjugated to a range of ... Creative Biolabs has developed a unique protein and antibody site-specific biotinylation platform named as BtAP-Tag® that well ...
  • Using this device, we will optimize the mechanical stimulation (thefrequency, the magnitude and the duration of substrate stretch) based on cell morphology, the organization ofthe actin cytoskeleton, and the extent of biotinylation. (elsevier.com)
  • The force-dependent change in the biotinylation profile is an indicationof altered protein complexes. (elsevier.com)
  • The One-Step Antibody Biotinylation Kit is optimized for the rapid and simple biotinylation of antibodies. (miltenyibiotec.com)
  • With the One-Step Antibody Biotinylation Kit, 10 μg of CD15 (A) and CD4 (B) antibodies were biotinylated as described. (miltenyibiotec.com)
  • The One-Step Antibody Biotinylation Kit has been developed for the biotinylation of monoclonal antibodies for use in magnetic cell separation (with MACS® Technology) as well as fluorescent cell analysis. (miltenyibiotec.com)
  • The variety of biotinylation reagents with different functional group specificities is extremely useful, allowing one to choose a reagent that does not inactivate the target macromolecule. (thermofisher.com)
  • Biotinylate protein amines and maximize solubility of proteins with this long (29.0A) NHS-ester biotinylation reagent containing a pegylated, water-soluble spacer arm. (fishersci.no)
  • Applying this most popular biotinylation reagent, selective N-terminal biotinylation in the presence of lysine can be achieved by pH-control (pH ca. 6.5). (clinicaltrialsarena.com)
  • When using chemical biotinylation, a number of factors of the biotinylation reagent must be carefully considered and optimized, such as solubility, spacer arm length, and cleavability. (biologicscorp.com)
  • Solubility: The solubility of the biotinylation reagent can be modified (such as by adding a polyethylene glycol spacer arm) to access hydrophobic or hydrophilic regions within the target protein or antibody and influence its solubility. (biologicscorp.com)
  • An amine reactive, photocleavable biotinylation reagent. (clickchemistrytools.com)
  • 4. A method for producing Cypridina luciferase wherein a sugar chain moiety has been biotinylated, comprising a step of introducing an aldehyde group in the sugar chain moiety by treating Cypridina luciferase having a sugar chain with a periodate salt and a step of subsequently reacting the aldehyde group in Cypridina luciferase having the sugar chain with a biotinylation reagent which selectively reacts with the aldehyde group. (freepatentsonline.com)
  • Enzymatic methods require the co-expression of bacterial biotin ligase and an exogenously expressed protein of interest that is modified to carry a biotin acceptor peptide, which provides a more uniform biotinylation than chemical methods and can be cell compartment specific. (thermofisher.com)
  • Schatz PJ (1993) Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli . (springer.com)
  • Biotinylation of a bioactive peptide allows its detection, isolation, enrichment or purification by affinity capture, albeit the incorporation of a biotin label lowers the solubility of the target compound. (clinicaltrialsarena.com)
  • Enzymatic biotinylation allows biotin to be linked at a single residue present in the protein/antibody, but it requires co-expression of bacterial biotin and modified antibody/protein to carry the acceptor peptide (usually a 15 amino acid peptide, termed AviTag). (biologicscorp.com)
  • Strikingly, biotinylation of GnRH under denaturing conditions largely abolished O-acylation, indicating that the observed O-biotinylation was dependent on peptide conformation. (elsevier.com)
  • 10 -10 M) and biotinylation of peptides is therefore an efficient method to specifically bind peptides to streptavidin coated surfaces. (pepscan.com)
  • Biotinylation of peptides can be performed either at the N- or C-terminus. (pepscan.com)
  • Besides building blocks for introducing the affinity tag including Fmoc-Lys(biotinyl)-OH coupled to Wang resin (D-2705), Bachem offers a vast choice of N-terminally biotinylated bioactive peptides as well as custom biotinylation. (clinicaltrialsarena.com)
  • In contrast, the biotinylation of selected peptides unrelated to GnRH under identical reaction conditions indicated no significant evidence of O- acylation of seryl residues. (elsevier.com)
  • Our platform employs phage genetically tagged for in vivo biotinylation during phage maturation that can easily be linked, through avidin, to any biotinylated affinity agent, including full-length antibodies, peptides, lectins or aptamers. (utmb.edu)
  • The One-Step Antibody Biotinylation Kit is optimized for the rapid and simple biotinylation of antibodies. (miltenyibiotec.com)
  • With the One-Step Antibody Biotinylation Kit, 10 μg of CD15 (A) and CD4 (B) antibodies were biotinylated as described. (miltenyibiotec.com)
  • The One-Step Antibody Biotinylation Kit has been developed for the biotinylation of monoclonal antibodies for use in magnetic cell separation (with MACS® Technology) as well as fluorescent cell analysis. (miltenyibiotec.com)
  • An ancestoral type enzyme AirID was designed from the sequence of biotinylation enzyme BirA of Escherichia coli by an ancestral enzyme reconstruction algorithm with metagenome data. (eurekalert.org)
  • Sulfo-NHS-LC-biotin is probably the most popular biotinylation currently available on the market. (timtec.net)
  • Further improvement of biotinylation enzymes is an important goal for enhancing the convenience of proximity biotinylation in cells. (eurekalert.org)
  • Recently, two new ligases termed TurboID and miniTurbo were developed using directed evolution of the BioID ligase and were able to produce robust biotinylation following a 10 min incubation with excess biotin. (mdpi.com)
  • However, TurboID enabled robust biotinylation in the endoplasmic reticulum lumen compared to BioID. (mdpi.com)
  • Biotinylation identification (BioID) is a unique and sensitive new method to screen for protein-protein interactions in living cells. (massachusettschronicle.com)
  • ProteoChem s biotinylation reagents are offered as water soluble (Sulfo-NHS ester containing) or insoluble varieties. (proteochem.com)
  • Biotinylation reagents along with LC linker (amino caproic acid) are a good illustration of dPEG excellent performance in comparison to its analog. (timtec.net)
  • Besides functional group specificity, biotinylation reagents are available with different solubility characteristics to focus biotinylation to distinct microenvironments either inside or outside cells. (thermofisher.com)
  • Wang J, Cantor AB, Orkin SH (2009) Tandem affinity purification of protein complexes in mouse embryonic stem cells using in vivo biotinylation. (springer.com)
  • However, there is reported concern about inducibility of biotinylation, cellular toxicity, and ligase stability. (mdpi.com)
  • Protein tags may allow specific enzymatic modification (such as biotinylation by biotin ligase) or chemical modification (such as reaction with FlAsH-EDT2 for fluorescence imaging). (wikipedia.org)
  • Biotinylation reagents are widely used to enable the isolation, separation, concentration and further downstream processing or analysis of biomolecules. (proteochem.com)
  • When the R domain of CFTR was expressed in the cytosol of BHK (baby-hamster kidney) cells as a soluble polypeptide it was also labelled after surface biotinylation and pulled down on streptavidin beads. (biochemj.org)
  • These results suggest that there is weak surface expression of immature ΔF508-CFTR on airway epithelial cells and demonstrate the need to remove permeable cells when studying CFTR glycoforms by surface biotinylation. (biochemj.org)
  • ET-1 did not alter total or plasma membrane-localized TRPC3, as determined using surface biotinylation. (ahajournals.org)
  • Here we used molecular modelling to produce a range of ligand binding domain (LBD) point mutants of GluK1-3 KAR subunits with and without altered agonist efficacy to further investigate the role of glutamate binding in surface trafficking and activation of homomeric and heteromeric KARs using endoglycosidase digestion, cell surface biotinylation and imaging of changes in intracellular Ca 2+ concentration [Ca 2+ ] i . (springer.com)
  • We have determined the distribution of NHE1 by means of immunofluorescence microscopy and cell-surface biotinylation. (biochemj.org)
  • Surface biotinylation of ENaC demonstrated an increase in channel number in the apical membrane following cAMP stimulation. (rupress.org)
  • Mass spectrometric analyses established the stoichiometry of biotinylation and confirmed that substantial O-biotinylation of residue Ser 4 , and to a minor extent Tyr 5 , of GnRH and the two analogs had occurred. (elsevier.com)
  • Biotinylation, also called biotin labeling, is most commonly performed through chemical means, although enzymatic methods are also available. (thermofisher.com)
  • However, the conventional labeling period requires 15-18 h for robust biotinylation which may not be ideal for some applications. (mdpi.com)
  • For TurboID we observed signs of protein instability, persistent biotinylation in the absence of exogenous biotin, and an increase in the practical labeling radius. (mdpi.com)
  • Here, using biotinylation, immunofluorescence resonance energy transfer (immunoFRET) microscopy, and RNAi-mediated knockdown, we demonstrate that rab4A-positive early endosomes traffic BKα to the plasma membrane in myocytes of resistance-size cerebral arteries. (physiology.org)
  • Chemical methods provide greater flexibility in the type of biotinylation needed than enzymatic approaches and can be performed both in vitro and in vivo . (thermofisher.com)
  • Biotinylation reagents are available for targeting specific functional groups or residues, including primary amines, sulfhydryls, carboxyls and carbohydrates. (thermofisher.com)
  • ProteoChem manufactures an assortment of biotinylation reagents that target various functional groups like primary amines, sulfhydryls (thiols), carboxyls, and carbohydrates. (proteochem.com)
  • In order to efficiently biotinylate a sample, biotinylation solution should be used at a 15-fold molar excess over the amount of amine-containing protein. (tcichemicals.com)
  • These studies provide unambiguous evidence that biotinylation is a natural, albeit rare, histone modification. (nih.gov)
  • Holocarboxylase synthetase (HCS) catalyzes the binding of the vitamin biotin to histones H3 and H4, thereby creating rare histone biotinylation marks in the epigenome. (nebraska.edu)
  • The occurrence of O-acylation during biotinylation of gonadotropin- releasing hormone and analogs. (elsevier.com)
  • In this research, we designed ancestral biotinylation enzymes using an ancestral enzyme reconstruction algorithm and metagenome data. (eurekalert.org)
  • Thus, the lower activity of MCCase in leaves is attributed to the reduced biotinylation of the biotin-containing subunit of the enzyme. (plantphysiol.org)
  • Our ReadiLink™ Protein Biotinylation Kit is optimized for the preparation of biotin-labeled IgG for enzyme immunoassay (EIA). (aatbio.com)
  • Traditional biotinylation involves either the direct coupling of biotin to a target molecule or the coupling of biotin to a spacer molecule such as lysine (forming biocytin ), aminocaproic acid, an aliphatic diamine ( e.g., butylene diamine, hexylene diamine), or some similar linker, followed by coupling of the biotin-spacer conjugate to the biomolecule of interest. (quantabiodesign.com)
  • Kim J, Cantor AB, Orkin SH, Wang J (2009) Use of in vivo biotinylation to study protein-protein and protein-DNA interactions in mouse embryonic stem cells. (springer.com)
  • Intracellular biotinylation was reduced when cells were treated with sulfo-NHS-LC-biotin (biotin attached to a reactive NHS ester with an aminocaproic acid spacer) or sulfo-NHS-PEO 12 -biotin [biotin attached to a reactive NHS ester with a poly(ethylene glycol) spacer], but the reduction could be explained by the lower reactivity of these reagents. (biochemj.org)
  • Biotinylation at the N-terminus can be performed directly to the primary-terminal amino group, whereas biotinylation is usually performed at the ε-amino group of an (extra) C-terminal lysine. (pepscan.com)
  • Biotinylation is a natural, albeit rare, modification of human histones. (nih.gov)
  • Recently, a team of investigators failed to detect biotinylated histones and proposed that biotinylation is not a natural modification of histones, but rather an assay artifact. (nih.gov)
  • The force-dependent change in the biotinylation profile is an indicationof altered protein complexes. (elsevier.com)
  • Reaction of the biotinylated derivatives with hydroxylamine indicated that significant O-biotinylation had occurred. (elsevier.com)
  • Using this device, we will optimize the mechanical stimulation (thefrequency, the magnitude and the duration of substrate stretch) based on cell morphology, the organization ofthe actin cytoskeleton, and the extent of biotinylation. (elsevier.com)
  • We conclude that physical interactions between HCS and EHMT1 mediate epigenomic synergies between biotinylation and methylation events. (nebraska.edu)