A member of the annexin family that is a substrate for a tyrosine kinase, ONCOGENE PROTEIN PP60(V-SRC). Annexin A2 occurs as a 36-KDa monomer and in a 90-KDa complex containing two subunits of annexin A2 and two subunits of S100 FAMILY PROTEIN P11. The monomeric form of annexin A2 was formerly referred to as calpactin I heavy chain.
Protein of the annexin family exhibiting lipid interaction and steroid-inducibility.
A protein of the annexin family isolated from human PLACENTA and other tissues. It inhibits cytosolic PHOSPHOLIPASE A2, and displays anticoagulant activity.
Protein of the annexin family with a probable role in exocytotic and endocytotic membrane events.
Protein of the annexin family originally isolated from the electric organ of the electric ray Torpedo marmorata. It has been found in a wide range of mammalian tissue where it is localized to the apical membrane of polarized EPITHELIAL CELLS.
An annexin family member that plays a role in MEMBRANE FUSION and signaling via VOLTAGE-DEPENDENT CALCIUM CHANNELS.
A protein of the annexin family that catalyzes the conversion of 1-D-inositol 1,2-cyclic phosphate and water to 1-D-myo-inositol 1-phosphate.
Family of calcium- and phospholipid-binding proteins which are structurally related and exhibit immunological cross-reactivity. Each member contains four homologous 70-kDa repeats. The annexins are differentially distributed in vertebrate tissues (and lower eukaryotes) and appear to be involved in MEMBRANE FUSION and SIGNAL TRANSDUCTION.
A family of highly acidic calcium-binding proteins found in large concentration in the brain and believed to be glial in origin. They are also found in other organs in the body. They have in common the EF-hand motif (EF HAND MOTIFS) found on a number of calcium binding proteins. The name of this family derives from the property of being soluble in a 100% saturated ammonium sulfate solution.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Quaternary ammonium analog of ethidium; an intercalating dye with a specific affinity to certain forms of DNA and, used as diiodide, to separate them in density gradients; also forms fluorescent complexes with cholinesterase which it inhibits.
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.
Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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.
A cell line derived from cultured tumor cells.
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.
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.
Technique using an instrument system for making, processing, and displaying one or more measurements on individual cells obtained from a cell suspension. Cells are usually stained with one or more fluorescent dyes specific to cell components of interest, e.g., DNA, and fluorescence of each cell is measured as it rapidly transverses the excitation beam (laser or mercury arc lamp). Fluorescence provides a quantitative measure of various biochemical and biophysical properties of the cell, as well as a basis for cell sorting. Other measurable optical parameters include light absorption and light scattering, the latter being applicable to the measurement of cell size, shape, density, granularity, and stain uptake.
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.
Extracellular vesicles generated by the shedding of CELL MEMBRANE blebs.
A family of G-protein-coupled receptors that was originally identified by its ability to bind N-formyl peptides such as N-FORMYLMETHIONINE LEUCYL-PHENYLALANINE. Since N-formyl peptides are found in MITOCHONDRIA and BACTERIA, this class of receptors is believed to play a role in mediating cellular responses to cellular damage and bacterial invasion. However, non-formylated peptide ligands have also been found for this receptor class.
Proteins prepared by recombinant DNA technology.
A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.
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.
Organic compounds that contain technetium as an integral part of the molecule. These compounds are often used as radionuclide imaging agents.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.
Established cell cultures that have the potential to propagate indefinitely.
A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.
Fluorescent probe capable of being conjugated to tissue and proteins. It is used as a label in fluorescent antibody staining procedures as well as protein- and amino acid-binding techniques.
An in situ method for detecting areas of DNA which are nicked during APOPTOSIS. Terminal deoxynucleotidyl transferase is used to add labeled dUTP, in a template-independent manner, to the 3 prime OH ends of either single- or double-stranded DNA. The terminal deoxynucleotidyl transferase nick end labeling, or TUNEL, assay labels apoptosis on a single-cell level, making it more sensitive than agarose gel electrophoresis for analysis of DNA FRAGMENTATION.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
The parts of a macromolecule that directly participate in its specific combination with another molecule.

HIV-1 Gag shares a signature motif with annexin (Anx7), which is required for virus replication. (1/67)

Genetic and biochemical analyses of the Gag protein of HIV-1 indicate a crucial role for this protein in several functions related to viral replication, including viral assembly. It has been suggested that Gag may fulfill some of the functions by recruiting host cellular protein(s). In our effort to identify structural and functional homologies between Gag and cellular cytoskeletal and secretory proteins involved in transport, we observed that HIV-1 Gag contains a unique PGQM motif in the capsid region. This motif was initially noted in the regulatory domain of synexin the membrane fusion protein of Xenopus laevis. To evaluate the functional significance of the highly conserved PGQM motif, we introduced alanine (A) in place of individual residues of the PGQM and deleted the motif altogether in a Gag expression plasmid and in an HIV-1 proviral DNA. The proviral DNA containing mutations in the PGQM motif showed altered expression, assembly, and release of viral particles in comparison to parental (NL4-3) DNA. When tested in multiple- and single-round replication assays, the mutant viruses exhibited distinct replication phenotypes; the viruses containing the A for the G and Q residues failed to replicate, whereas A in place of the P and M residues did not inhibit viral replication. Deletion of the tetrapeptide also resulted in the inhibition of replication. These results suggest that the PGQM motif may play an important role in the infection process of HIV-1 by facilitating protein-protein interactions between viral and/or viral and cellular proteins.  (+info)

Annexin VII and annexin XI are tyrosine phosphorylated in peroxovanadate-treated dogs and in platelet-derived growth factor-treated rat vascular smooth muscle cells. (2/67)

The intraperitoneal administration of peroxovanadate results in the rapid accumulation of many tyrosine-phosphorylated proteins in the liver and kidney of treated animals. The availability of large pools of tyrosine-phosphorylated proteins derived from normal tissues facilitates the purification and identification of previously unknown targets for cellular tyrosine kinases. Using this procedure, we have thus far identified four proteins in the liver and kidney of peroxovanadate-treated dogs. Two of these, annexin VII and annexin XI, were novel and had not been previously reported to be substrates of tyrosine kinases while the remaining two, ezrin and clathrin, have been reported to be tyrosine phosphorylated in some cell culture systems. In the present study, isolated proteins were identified both by sequence analysis and immunological methods. Annexin VII and annexin XI are present in cultured rat vascular smooth muscle cells and both were tyrosine phosphorylated in response to a physiological ligand, platelet-derived growth factor-BB (PDGF-BB). Furthermore, the extent of tyrosine phosphorylation in response to PDGF-BB was augmented by the co-addition of peroxovanadate to cell cultures. In vitro phosphorylation assays showed that PDGF receptor, calcium-dependent tyrosine kinase (CADTK/Pyk-2), Src kinase, and epidermal growth factor receptor all were able to phosphorylate purified annexin VII and XI on tyrosine residues. These findings confirm the usefulness of phosphatase inhibition by peroxovanadate as a tool for identifying previously unknown physiological targets for cellular protein tyrosine kinases.  (+info)

Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse. (3/67)

The mammalian anx7 gene codes for a Ca(2+)-activated GTPase, which supports Ca(2+)/GTP-dependent secretion events and Ca(2+) channel activities in vitro and in vivo. To test whether anx7 might be involved in Ca(2+) signaling in secreting pancreatic beta cells, we knocked out the anx7 gene in the mouse and tested the insulin-secretory properties of the beta cells. The nullizygous anx7 (-/-) phenotype is lethal at embryonic day 10 because of cerebral hemorrhage. However, the heterozygous anx7 (+/-) mouse, although expressing only low levels of ANX7 protein, is viable and fertile. The anx7 (+/-) phenotype is associated with a substantial defect in insulin secretion, although the insulin content of the islets, is 8- to 10-fold higher in the mutants than in the normal littermate control. We infer from electrophysiological studies that both glucose-stimulated secretion and voltage-dependent Ca(2+) channel functions are normal. However, electrooptical recordings indicate that the (+/-) mutation has caused a change in the ability of inositol 1,4,5-trisphosphate (IP(3))-generating agonists to release intracellular calcium. The principle molecular consequence of lower anx7 expression is a profound reduction in IP(3) receptor expression and function in pancreatic islets. The profound increase in islets, beta cell number, and size may be a means of compensating for less efficient insulin secretion by individual defective pancreatic beta cells. This is a direct demonstration of a connection between glucose-activated insulin secretion and Ca(2+) signaling through IP(3)-sensitive Ca(2+) stores.  (+info)

Annexins VII and XI are present in a human macrophage-like cell line. Differential translocation on FcR-mediated phagocytosis. (4/67)

We have studied the divalent cation-dependent association of proteins to subcellular fractions of human macrophage-like cells before and after FcR-mediated phagocytosis. Among these proteins we have identified annexins VII and XI for the first time in these cells, along with annexins I, III, and VI. Although all of these annexins are present in the cytosolic fraction, the extent of their association to membrane and phagosome fractions from resting and stimulated cells is variable. Annexin VII translocates from cytosolic to membrane fractions after phagocytic stimulation, along with annexin I, III, and VI. Annexins VII and XI are found associated with purified phagosomes along with I, III, and VI, and this association is greater after a 24-h chase period. Our results show differences in the intracellular distribution of different annexins in macrophage-like cells on phagocytosis. Annexins VII, VI, III, and I respond to particle ingestion by translocating to phagosomes and other cell membrane structures, whereas annexin XI translocates predominantly to phagosomes, suggesting dissimilarities in their function.  (+info)

The sorcin-annexin VII calcium-dependent interaction requires the sorcin N-terminal domain. (5/67)

Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. In turn, the lack of complex formation between the sorcin Ca(2+) binding domain (33-198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182-22190]. The interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.  (+info)

The annexinopathies: a new category of diseases. (6/67)

The annexins are a family of highly homologous phospholipid binding proteins, which share a four-domain structure, with one member of the family - annexin VI - having a duplication consisting of eight domains. Thus far, ten annexins have been described in mammals. Although the biological functions of the annexins have not been definitively established, two human diseases involving annexin abnormalities ('annexinopathies') have been identified as of the time of writing. Overexpression of annexin II occurs in the leukocytes of a subset of patients having a hemorrhagic form of acute promyelocytic leukemia. Underexpression of annexin V occurs on placental trophoblasts in the antiphospholipid syndrome and in preeclampsia. Also, an animal model has been described in which annexin VII is underexpressed and is associated with disease, but the relevance of this animal model to human disease is not yet understood. Future research is likely to elucidate additional 'annexinopathies'.  (+info)

Activation of annexin 7 by protein kinase C in vitro and in vivo. (7/67)

Annexin 7, a Ca(2+)/GTP-activated membrane fusion protein, is preferentially phosphorylated in intact chromaffin cells, and the levels of annexin 7 phosphorylation increase quantitatively in proportion to the extent of catecholamine secretion. Consistently, various protein kinase C inhibitors proportionately reduce both secretion and phosphorylation of annexin 7 in these cells. In vitro, annexin 7 is quantitatively phosphorylated by protein kinase C to a mole ratio of 2.0, and phosphorylation is extraordinarily sensitive to variables such as pH, calcium, phospholipid, phorbol ester, and annexin 7 concentration. Phosphorylation of annexin 7 by protein kinase C significantly potentiates the ability of the protein to fuse phospholipid vesicles and lowers the half-maximal concentration of calcium needed for this fusion process. Furthermore, other protein kinases, including cAMP-dependent protein kinase, cGMP-dependent protein kinase, and protein-tyrosine kinase pp60(c-)(src), also label annexin 7 with high efficiency but do not have this effect on membrane fusion. In the case of pp60(c-)(src), we note that this kinase, if anything, modestly suppresses the membrane fusion activity of annexin 7. These results thus lead us to hypothesize that annexin 7 may be a positive mediator for protein kinase C action in the exocytotic membrane fusion reaction in chromaffin cells.  (+info)

ANX7, a candidate tumor suppressor gene for prostate cancer. (8/67)

The ANX7 gene is located on human chromosome 10q21, a site long hypothesized to harbor a tumor suppressor gene(s) (TSG) associated with prostate and other cancers. To test whether ANX7 might be a candidate TSG, we examined the ANX7-dependent suppression of human tumor cell growth, stage-specific ANX7 expression in 301 prostate specimens on a prostate tissue microarray, and loss of heterozygosity (LOH) of microsatellite markers at or near the ANX7 locus. Here we report that human tumor cell proliferation and colony formation are markedly reduced when the wild-type ANX7 gene is transfected into two prostate tumor cell lines, LNCaP and DU145. Consistently, analysis of ANX7 protein expression in human prostate tumor microarrays reveals a significantly higher rate of loss of ANX7 expression in metastatic and local recurrences of hormone refractory prostate cancer as compared with primary tumors (P = 0.0001). Using four microsatellite markers at or near the ANX7 locus, and laser capture microdissected tumor cells, 35% of the 20 primary prostate tumors show LOH. The microsatellite marker closest to the ANX7 locus showed the highest rate of LOH, including one homozygous deletion. We conclude that the ANX7 gene exhibits many biological and genetic properties expected of a TSG and may play a role in prostate cancer progression.  (+info)

Annexin A2 is a protein found in various types of cells, including those that line the inside of blood vessels. It is a member of the annexin family of proteins, which are characterized by their ability to bind to calcium ions and membranes. Annexin A2 is involved in several cellular processes, including the regulation of ion channels, the modulation of enzyme activity, and the promotion of cell adhesion and migration. It also plays a role in the coagulation of blood, and has been implicated in the development and progression of various diseases, including cancer and cardiovascular disease.

Annexin A1 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. This protein is found in various tissues, including the human body, and has multiple functions, such as anti-inflammatory, anti-proliferative, and pro-resolving activities. It plays a crucial role in regulating cellular processes like apoptosis (programmed cell death), membrane organization, and signal transduction.

Annexin A1 is also known to interact with other proteins and receptors, such as the formyl peptide receptor 2 (FPR2), which contributes to its immunomodulatory functions. In addition, it has been implicated in several pathophysiological conditions, including cancer, inflammation, and autoimmune diseases.

Modulating Annexin A1 levels or activity may provide therapeutic benefits for various medical conditions; however, further research is required to fully understand its potential as a drug target.

Annexin A5 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. Annexin A5 has high affinity for phosphatidylserine, a type of phospholipid that is usually located on the inner leaflet of the plasma membrane in healthy cells. However, when cells undergo apoptosis (programmed cell death), phosphatidylserine is exposed on the outer leaflet of the plasma membrane.

Annexin A5 can bind to exposed phosphatidylserine on the surface of apoptotic cells and is commonly used as a marker for detecting apoptosis in various experimental settings, including flow cytometry, immunohistochemistry, and imaging techniques. Annexin A5-based assays are widely used in research and clinical settings to study the mechanisms of apoptosis and to develop diagnostic tools for various diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases.

Annexin A6 is a protein that belongs to the annexin family, which are calcium-dependent phospholipid-binding proteins. Annexin A6 is involved in various cellular processes such as exocytosis, endocytosis, and membrane trafficking. It has been shown to play a role in regulating ion channels, modulating the actin cytoskeleton, and interacting with other proteins to form multimolecular complexes. Annexin A6 is expressed in various tissues, including the heart, lung, kidney, and pancreas. Mutations in the ANXA6 gene have been associated with certain diseases, such as kidney stones and cataracts.

Annexin A4 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to calcium ions and membranes. Specifically, Annexin A4 is known to play roles in various cellular processes such as exocytosis, endocytosis, and regulation of ion channels. It has also been implicated in the development and progression of certain diseases, including cancer and neurological disorders.

In the medical field, the study of Annexin A4 is important for understanding its functions and potential therapeutic applications. For example, research has suggested that targeting Annexin A4 may be a useful strategy for developing new treatments for cancer or other diseases. However, more studies are needed to fully elucidate the role of this protein in various biological processes and disease states.

Annexin A7 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to cell membranes in a calcium-dependent manner. Specifically, Annexin A7 (also known as Syntaxin-binding protein 1 or SBP1) is involved in various cellular processes such as exocytosis, endocytosis, and signal transduction. It has been shown to interact with other proteins, including syntaxins, which are important for vesicle trafficking and fusion. Additionally, Annexin A7 may have a role in regulating apoptosis (programmed cell death) and has been implicated in several diseases, including cancer and neurodegenerative disorders. However, more research is needed to fully understand the functions and regulatory mechanisms of this protein.

Annexin A3 is a type of protein that belongs to the annexin family, which are characterized by their ability to bind to calcium ions and membranes. Specifically, annexin A3 is involved in various cellular processes such as exocytosis, endocytosis, and signal transduction. It has been found to play a role in the regulation of blood clotting, inflammation, and cancer metastasis. Annexin A3 can be found on the surface of various cells, including platelets, neutrophils, and tumor cells. In addition, annexin A3 has been identified as a potential biomarker for certain types of cancer, such as ovarian and prostate cancer.

Annexins are a family of calcium-dependent phospholipid-binding proteins that are found in various organisms, including humans. They are involved in several cellular processes, such as membrane organization, signal transduction, and regulation of ion channels. Some annexins also have roles in inflammation, blood coagulation, and apoptosis (programmed cell death).

Annexins have a conserved structure, consisting of a core domain that binds to calcium ions and a variable number of domains that bind to phospholipids. This allows annexins to interact with membranes in a calcium-dependent manner, which is important for their functions.

There are several different annexin proteins, each with its own specific functions and expression patterns. For example, annexin A1 is involved in the regulation of inflammation and has been studied as a potential target for anti-inflammatory therapies. Annexin A2 is involved in the regulation of coagulation and has been studied as a potential target for anticoagulant therapies. Other annexins have roles in cell division, differentiation, and survival.

Overall, annexins are important regulators of various cellular processes and have potential as targets for therapeutic intervention in a variety of diseases.

S100 proteins are a family of calcium-binding proteins that are involved in the regulation of various cellular processes, including cell growth and differentiation, intracellular signaling, and inflammation. They are found in high concentrations in certain types of cells, such as nerve cells (neurons), glial cells (supporting cells in the nervous system), and skin cells (keratinocytes).

The S100 protein family consists of more than 20 members, which are divided into several subfamilies based on their structural similarities. Some of the well-known members of this family include S100A1, S100B, S100 calcium-binding protein A8 (S100A8), and S100 calcium-binding protein A9 (S100A9).

Abnormal expression or regulation of S100 proteins has been implicated in various pathological conditions, such as neurodegenerative diseases, cancer, and inflammatory disorders. For example, increased levels of S100B have been found in the brains of patients with Alzheimer's disease, while overexpression of S100A8 and S100A9 has been associated with the development and progression of certain types of cancer.

Therefore, understanding the functions and regulation of S100 proteins is important for developing new diagnostic and therapeutic strategies for various diseases.

Phosphatidylserines are a type of phospholipids that are essential components of the cell membrane, particularly in the brain. They play a crucial role in maintaining the fluidity and permeability of the cell membrane, and are involved in various cellular processes such as signal transduction, protein anchorage, and apoptosis (programmed cell death). Phosphatidylserines contain a polar head group made up of serine amino acids and two non-polar fatty acid tails. They are abundant in the inner layer of the cell membrane but can be externalized to the outer layer during apoptosis, where they serve as signals for recognition and removal of dying cells by the immune system. Phosphatidylserines have been studied for their potential benefits in various medical conditions, including cognitive decline, Alzheimer's disease, and depression.

Apoptosis is a programmed and controlled cell death process that occurs in multicellular organisms. It is a natural process that helps maintain tissue homeostasis by eliminating damaged, infected, or unwanted cells. During apoptosis, the cell undergoes a series of morphological changes, including cell shrinkage, chromatin condensation, and fragmentation into membrane-bound vesicles called apoptotic bodies. These bodies are then recognized and engulfed by neighboring cells or phagocytic cells, preventing an inflammatory response. Apoptosis is regulated by a complex network of intracellular signaling pathways that involve proteins such as caspases, Bcl-2 family members, and inhibitors of apoptosis (IAPs).

Propidium is not a medical condition or diagnosis, but rather it is a fluorescent dye that is used in medical and scientific research. It is often used in procedures such as flow cytometry and microscopy to stain and label cells or nucleic acids (DNA or RNA). Propidium iodide is the most commonly used form of propidium, which binds to DNA by intercalating between the bases.

Once stained with propidium iodide, cells with damaged membranes will take up the dye and can be detected and analyzed based on their fluorescence intensity. This makes it possible to identify and quantify dead or damaged cells in a population, as well as to analyze DNA content and cell cycle status.

Overall, propidium is an important tool in medical research and diagnostics, providing valuable information about cell health, viability, and genetic material.

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.

Phospholipids are a major class of lipids that consist of a hydrophilic (water-attracting) head and two hydrophobic (water-repelling) tails. The head is composed of a phosphate group, which is often bound to an organic molecule such as choline, ethanolamine, serine or inositol. The tails are made up of two fatty acid chains.

Phospholipids are a key component of cell membranes and play a crucial role in maintaining the structural integrity and function of the cell. They form a lipid bilayer, with the hydrophilic heads facing outwards and the hydrophobic tails facing inwards, creating a barrier that separates the interior of the cell from the outside environment.

Phospholipids are also involved in various cellular processes such as signal transduction, intracellular trafficking, and protein function regulation. Additionally, they serve as emulsifiers in the digestive system, helping to break down fats in the diet.

Calcium-binding proteins (CaBPs) are a diverse group of proteins that have the ability to bind calcium ions (Ca^2+^) with high affinity and specificity. They play crucial roles in various cellular processes, including signal transduction, muscle contraction, neurotransmitter release, and protection against oxidative stress.

The binding of calcium ions to these proteins induces conformational changes that can either activate or inhibit their functions. Some well-known CaBPs include calmodulin, troponin C, S100 proteins, and parvalbumins. These proteins are essential for maintaining calcium homeostasis within cells and for mediating the effects of calcium as a second messenger in various cellular signaling pathways.

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.

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.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

"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.

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.

Flow cytometry is a medical and research technique used to measure physical and chemical characteristics of cells or particles, one cell at a time, as they flow in a fluid stream through a beam of light. The properties measured include:

* Cell size (light scatter)
* Cell internal complexity (granularity, also light scatter)
* Presence or absence of specific proteins or other molecules on the cell surface or inside the cell (using fluorescent antibodies or other fluorescent probes)

The technique is widely used in cell counting, cell sorting, protein engineering, biomarker discovery and monitoring disease progression, particularly in hematology, immunology, and cancer research.

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.

Cell-derived microparticles (CDMs), also known as microvesicles or microparticles, are small membrane-bound particles that are released from the cell surface upon activation or apoptosis of various cell types, including platelets, leukocytes, endothelial cells, and red blood cells. CDMs range in size from 0.1 to 1.0 micrometers in diameter and contain a variety of bioactive molecules, such as lipids, proteins, and nucleic acids, which can be transferred to neighboring or distant cells, thereby modulating their function.

CDMs have been implicated in various physiological and pathological processes, including coagulation, inflammation, immune response, angiogenesis, and cancer progression. They have also emerged as potential biomarkers for various diseases, such as cardiovascular disease, sepsis, and cancer, due to their distinct molecular signature and abundance in body fluids, such as blood, urine, and cerebrospinal fluid.

The mechanisms of CDM formation and release are complex and involve several cellular processes, including cytoskeletal rearrangement, membrane budding, and vesicle shedding. The molecular composition of CDMs reflects their cellular origin and activation state, and can be analyzed by various techniques, such as flow cytometry, proteomics, and transcriptomics, to gain insights into their biological functions and clinical relevance.

Formyl peptide receptors (FPRs) are a type of G protein-coupled receptors that play a crucial role in the innate immune system. They are expressed on various cells including neutrophils, monocytes, and macrophages. FPRs recognize and respond to formylated peptides derived from bacteria, mitochondria, and host proteins during cell damage or stress. Activation of FPRs triggers a variety of cellular responses, such as chemotaxis, phagocytosis, and release of inflammatory mediators, which help to eliminate invading pathogens and promote tissue repair. There are three subtypes of human FPRs (FPR1, FPR2, and FPR3) that have distinct ligand specificities and functions in the immune response.

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.

Caspase-3 is a type of protease enzyme that plays a central role in the execution-phase of cell apoptosis, or programmed cell death. It's also known as CPP32 (CPP for ced-3 protease precursor) or apopain. Caspase-3 is produced as an inactive protein that is activated when cleaved by other caspases during the early stages of apoptosis. Once activated, it cleaves a variety of cellular proteins, including structural proteins, enzymes, and signal transduction proteins, leading to the characteristic morphological and biochemical changes associated with apoptotic cell death. Caspase-3 is often referred to as the "death protease" because of its crucial role in executing the cell death program.

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.

Organotechnetium compounds are chemical substances that contain carbon-technetium bonds, where technetium is an element with the symbol Tc and atomic number 43. These types of compounds are primarily used in medical imaging as radioactive tracers due to the ability of technetium-99m to emit gamma rays. The organotechnetium compounds help in localizing specific organs, tissues, or functions within the body, making them useful for diagnostic purposes in nuclear medicine.

It is important to note that most organotechnetium compounds are synthesized from technetium-99m, which is generated from the decay of molybdenum-99. The use of these compounds requires proper handling and administration by trained medical professionals due to their radioactive nature.

Cell survival refers to the ability of a cell to continue living and functioning normally, despite being exposed to potentially harmful conditions or treatments. This can include exposure to toxins, radiation, chemotherapeutic drugs, or other stressors that can damage cells or interfere with their normal processes.

In scientific research, measures of cell survival are often used to evaluate the effectiveness of various therapies or treatments. For example, researchers may expose cells to a particular drug or treatment and then measure the percentage of cells that survive to assess its potential therapeutic value. Similarly, in toxicology studies, measures of cell survival can help to determine the safety of various chemicals or substances.

It's important to note that cell survival is not the same as cell proliferation, which refers to the ability of cells to divide and multiply. While some treatments may promote cell survival, they may also inhibit cell proliferation, making them useful for treating diseases such as cancer. Conversely, other treatments may be designed to specifically target and kill cancer cells, even if it means sacrificing some healthy cells in the process.

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.

Caspases are a family of protease enzymes that play essential roles in programmed cell death, also known as apoptosis. These enzymes are produced as inactive precursors and are activated when cells receive signals to undergo apoptosis. Once activated, caspases cleave specific protein substrates, leading to the characteristic morphological changes and DNA fragmentation associated with apoptotic cell death. Caspases also play roles in other cellular processes, including inflammation and differentiation. There are two types of caspases: initiator caspases (caspase-2, -8, -9, and -10) and effector caspases (caspase-3, -6, and -7). Initiator caspases are activated in response to various apoptotic signals and then activate the effector caspases, which carry out the proteolytic cleavage of cellular proteins. Dysregulation of caspase activity has been implicated in a variety of diseases, including neurodegenerative disorders, ischemic injury, and cancer.

Fluorescein-5-isothiocyanate (FITC) is not a medical term per se, but a chemical compound commonly used in biomedical research and clinical diagnostics. Therefore, I will provide a general definition of this term:

Fluorescein-5-isothiocyanate (FITC) is a fluorescent dye with an absorption maximum at approximately 492-495 nm and an emission maximum at around 518-525 nm. It is widely used as a labeling reagent for various biological molecules, such as antibodies, proteins, and nucleic acids, to study their structure, function, and interactions in techniques like flow cytometry, immunofluorescence microscopy, and western blotting. The isothiocyanate group (-N=C=S) in the FITC molecule reacts with primary amines (-NH2) present in biological molecules to form a stable thiourea bond, enabling specific labeling of target molecules for detection and analysis.

In situ nick-end labeling (ISEL, also known as TUNEL) is a technique used in pathology and molecular biology to detect DNA fragmentation, which is a characteristic of apoptotic cells (cells undergoing programmed cell death). The method involves labeling the 3'-hydroxyl termini of double or single stranded DNA breaks in situ (within tissue sections or individual cells) using modified nucleotides that are coupled to a detectable marker, such as a fluorophore or an enzyme. This technique allows for the direct visualization and quantification of apoptotic cells within complex tissues or cell populations.

Fibrinolysin is defined as a proteolytic enzyme that dissolves or breaks down fibrin, a protein involved in the clotting of blood. This enzyme is produced by certain cells, such as endothelial cells that line the interior surface of blood vessels, and is an important component of the body's natural mechanism for preventing excessive blood clotting and maintaining blood flow.

Fibrinolysin works by cleaving specific bonds in the fibrin molecule, converting it into soluble degradation products that can be safely removed from the body. This process is known as fibrinolysis, and it helps to maintain the balance between clotting and bleeding in the body.

In medical contexts, fibrinolysin may be used as a therapeutic agent to dissolve blood clots that have formed in the blood vessels, such as those that can occur in deep vein thrombosis or pulmonary embolism. It is often administered in combination with other medications that help to enhance its activity and specificity for fibrin.

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.

... is a protein that in humans is encoded by the ANXA7 gene. Annexin VII is a member of the annexin family of calcium- ... "Entrez Gene: ANXA7 annexin A7". Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 2002). "The penta-EF-hand ... "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent ... The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in ...
... annexin a5 MeSH D12.776.157.125.050.110 - annexin a6 MeSH D12.776.157.125.050.120 - annexin a7 MeSH D12.776.157.125.412.249 - ... annexin a1 MeSH D12.776.157.125.050.060 - annexin a2 MeSH D12.776.157.125.050.070 - Annexin A3 MeSH D12.776.157.125.050.080 - ...
Annexin A7 is a protein that in humans is encoded by the ANXA7 gene. Annexin VII is a member of the annexin family of calcium- ... "Entrez Gene: ANXA7 annexin A7". Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 2002). "The penta-EF-hand ... "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent ... The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in ...
Rabbit polyclonal antibody to Annexin VII (annexin A7). TA308796 Origene Technologies GmbH 100 µl. Ask for price ... Annexin I Rabbit Polyclonal Antibody. To Order: [email protected]. Annexin I Rabbit Polyclonal Antibody. ... Description: A polyclonal antibody for detection of Annexin I from Human. This Annexin I antibody is for WB, IF, IHC-P, ELISA. ... Description: A polyclonal antibody for detection of Annexin I from Human. This Annexin I antibody is for WB, IF, IHC-P, ELISA. ...
annexin A7. chaperonin containing TCP1, subunit 7 (eta). Image. No pdb structure. No pdb structure. ... annexin anticancer antitumor chinese cytotoxic cytotoxicity decreasing depressed dramatically eecp ethanol exerted explored ... annexin anticancer antitumor chinese cytotoxic cytotoxicity decreasing depressed dramatically eecp ethanol exerted explored ...
A7 promoted the cleavage of caspase-9 and caspase-3, as well as increased intracellular Ca levels and decreased the ... The population of Annexin-V positive/propidium iodide-negative cells also increased, indicating the induction of early ... N-tertbutyl-D-leucine-N-methyl-D-leucinebenzyl (A7), the only stereomer condensed by two D-leucines, showed the highest ... A7-treated cells showed cell cycle arrest and morphological changes typical of cells undergoing apoptosis. ...
... is linearly correlated with the uptake of the radio-labeled Annexin-V in the murine transplant tumors, showing that the Annexin ... metabolism 4.64 32726 116 PMF/TMS down A7 P43490 NAMPT Nicotinamide phosphoribosyltransferase metabolism 6.69 55772 57 TMS down ... indicated that the degree of radiation induced apoptosis in tumor could be represented by the99mTc-HYNIC- annexin V activity ... annexin V taken up by all tumors Guanylate cyclase 2C (ordinate), with a correlation coefficient (r) of 0.892 and a ...
Human ANXA7(Annexin A7) ELISA Kit. *Human AOPP(Advanced Oxidation Protein Products) ELISA Kit ...
Human ANXA7(Annexin A7) ELISA Kit. *Human AOPP(Advanced Oxidation Protein Products) ELISA Kit ...
Human ANXA7(Annexin A7) ELISA Kit. *Human AOPP(Advanced Oxidation Protein Products) ELISA Kit ...
Annexin V. Annexin A5. Annexin VI. Annexin A6. Annexin VII. Annexin A7. ... Annexin II. Annexin A2. Annexin IV. Annexin A4. ...
Annexin V. Annexin A5. Annexin VI. Annexin A6. Annexin VII. Annexin A7. ... Annexin II. Annexin A2. Annexin IV. Annexin A4. ...
Annexin V. Annexin A5. Annexin VI. Annexin A6. Annexin VII. Annexin A7. ... Annexin II. Annexin A2. Annexin IV. Annexin A4. ...
This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or [email protected] ...
Activation of a7 Nicotinic Acetylcholine Receptors Prevents Monosodium Iodoacetate-Induced Osteoarthritis in Rats Cellular ... The apoptotic rate was evaluated using an Annexin V-FITC apoptosis detection kit (eBioscience, San Diego, CA, USA) according to ... the cells were incubated in buffer containing FITC-annexin V and PI for 5 min at room temperature in the dark. Apoptotic cells ...
Human ANXA11(Annexin A11) ELISA Kit. *Human PPARd(Peroxisome Proliferator Activated Receptor Delta) ELISA Kit ... Human S100A7(S100 Calcium Binding Protein A7) ELISA Kit. *Human CDH17(Cadherin 17) ELISA Kit ...
In AML, elevated expression of HoxB3, B4, A7 11 is identified inside the most primitive progenitors with expression of A7 11 ... Cleaved PARP was identified in LY1 and LY8 cells by which apoptosis was detected by Annexin V PE 7AAD dual staining, though no ...
An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding. ... Barois A7, Brochier G8, Sternberg D9, Fournier E9, Hantaï D9, Abicht A10, Dusl M10, Laval SH2, Griffin H2, Eymard B9, ...
Human ANXA1(Annexin A1) ELISA Kit. * Human ANXA11(Annexin A11) ELISA Kit ... Human S100A7(S100 Calcium Binding Protein A7) ELISA Kit. * Human S100B(S100 Calcium Binding Protein B) ELISA Kit ...
Human ANXA1(Annexin A1) ELISA Kit. *Human ANXA11(Annexin A11) ELISA Kit ... Human S100A7(S100 Calcium Binding Protein A7) ELISA Kit. *Human S100B(S100 Calcium Binding Protein B) ELISA Kit ...
... coordinate induction of the transcription factor Sox9 and suppression of the proapoptotic phospholipid-binding protein Annexin ... EPH receptor A7 [Source:HGNC Sym.... A_52_P507537. 586. BCAT1. branched chain amino acid transa.... ...
Human Serpin A7 PicoKine ELISA Kit. *Human Serpin C1/Antithrombin-III PicoKine ELISA Kit ... Human Annexin A1 PicoKine ELISA Kit. *Human APOA1 PicoKine ELISA Kit. *Human APOE PicoKine ELISA Kit ...
Human ANXA10(Annexin A10) ELISA Kit. *Human ANXA9(Annexin A9) ELISA Kit ... Human RNASE7(Ribonuclease A7) ELISA Kit. *Human RNASE8(Ribonuclease A8) ELISA Kit ...
Human ANXA10(Annexin A10) ELISA Kit. *Human ANXA9(Annexin A9) ELISA Kit ... Human RNASE7(Ribonuclease A7) ELISA Kit. *Human RNASE8(Ribonuclease A8) ELISA Kit ...
UniProt ID A7. *UniProt ID A8. *UniProt ID A9. *UniProt ID B0 ... Annexin. *Aprotinin. *Avidin. *B Cell Lymphoma. *Beta 2 ...
Expression of annexin A7 and its clinical significance in gastric carcinoma].. Yuan HF; Li Y; Tan BB; Zhao Q; Fan LQ; Ye WH. ... 6. Annexin A7 is correlated with better clinical outcomes of patients with breast cancer.. Huang Y; Wang H; Yang Y. J Cell ... 8. Potential role of annexin A7 in cancers.. Guo C; Liu S; Greenaway F; Sun MZ. Clin Chim Acta; 2013 Aug; 423():83-9. PubMed ID ... 4. Annexin-A7 protects normal prostate cells and induces distinct patterns of RB-associated cytotoxicity in androgen-sensitive ...
Annexin A7 / biosynthesis* Actions. * Search in PubMed * Search in MeSH * Add to Search ... Annexin 7 mobilizes calcium from endoplasmic reticulum stores in brain. Watson WD, Srivastava M, Leighton X, Glasman M, Faraday ...
Calgranulins, annexins, S100 calcium-binding protein A7 and epidermal fatty acid-binding protein were abundant in CVF and ... annexin III); an anti-inflammatory cytokine (IL-1 receptor antagonist); proteinase inhibitors (A1AT, monocyte/neutrophil ...
Ubiquitin-protein ligase E3C promotes glioma progression by mediating the ubiquitination and degrading of Annexin A7. Pan SJ, ...
Annexin A7 Current Synonym true false 2537438012 Annexin VII Current Synonym true false ...
2005; see ANNEXIN VII 1993-2004; SYNEXIN was indexed under PROTEINS 1978-1992; ANNEXIN A7 was indexed under ANNEXIN VIII 2004. ... Annexin A7 Preferred Concept UI. M0026283. Registry Number. 0. Scope Note. An annexin family member that plays a role in ... Annexin A7 Preferred Term Term UI T570827. Date01/30/2004. LexicalTag NON. ThesaurusID NLM (2005). ... Annexin A7. Tree Number(s). D12.776.157.125.050.120. Unique ID. D017310. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
2005; see ANNEXIN VII 1993-2004; SYNEXIN was indexed under PROTEINS 1978-1992; ANNEXIN A7 was indexed under ANNEXIN VIII 2004. ... Annexin A7 Preferred Concept UI. M0026283. Registry Number. 0. Scope Note. An annexin family member that plays a role in ... Annexin A7 Preferred Term Term UI T570827. Date01/30/2004. LexicalTag NON. ThesaurusID NLM (2005). ... Annexin A7. Tree Number(s). D12.776.157.125.050.120. Unique ID. D017310. RDF Unique Identifier. http://id.nlm.nih.gov/mesh/ ...
2005; see ANNEXIN VII 1993-2004; SYNEXIN was indexed under PROTEINS 1978-1992; ANNEXIN A7 was indexed under ANNEXIN VIII 2004. ... Annexin A7 - Preferred Concept UI. M0026283. Scope note. An annexin family member that plays a role in MEMBRANE FUSION and ... An annexin family member that plays a role in MEMBRANE FUSION and signaling via VOLTAGE-DEPENDENT CALCIUM CHANNELS.. ...
annexin A7 [Source:HGNC Symbol;Acc:H.... BMI1. 648. BMI1. BMI1 proto-oncogene, polycomb ring f.... ...
Annexin A7. Below are MeSH descriptors whose meaning is more specific than "Annexin A4". ... Protein of the annexin family originally isolated from the electric organ of the electric ray Torpedo marmorata. It has been ... Annexin A4 reduces water and proton permeability of model membranes but does not alter aquaporin 2-mediated water transport in ... "Annexin A4" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ...
CST 3666S Annexin A7 Antibody 100µl ¥3,100 Cytoskeletal Signaling Polyclonal Antibody -20C ...
Annexin A2 N0000169588 Annexin A3 N0000169590 Annexin A4 N0000169589 Annexin A5 N0000169584 Annexin A6 N0000169586 Annexin A7 ... N0000169583 Annexins N0000170303 Anserine N0000171468 Ant Venoms N0000006006 Antazoline N0000179396 Antazoline Hydrochloride ... Anisoles N0000167149 Anisomycin N0000006251 Anistreplase N0000169316 Ankyrins N0000179042 annatto N0000169585 Annexin A1 ...
Furthermore, annexin A7 (ANXA7), p53, nuclear factor- κ B p65 (NF- κ B p65), reactive oxygen species (ROS) levels, and ...
Annexin V [P] MH NEW = Annexin A5 MH OLD = Annexin VI [P] MH NEW = Annexin A6 MH OLD = Annexin VII [P] MH NEW = Annexin A7 MH ... Annexin I [P] MH NEW = Annexin A1 MH OLD = Annexin II [P] MH NEW = Annexin A2 MH OLD = Annexin III [P] MH NEW = Annexin A3 MH ... OLD = Annexin IV [P] MH NEW = Annexin A4 MH OLD = ...
Human ANXA7(Annexin A7) ELISA Kit. *Human AOPP(Advanced Oxidation Protein Products) ELISA Kit ...
Human ANXA7(Annexin A7) ELISA Kit. *Human AOPP(Advanced Oxidation Protein Products) ELISA Kit ...
Annexin A1 Annexin A2 Annexin A3 Annexin A4 Annexin A5 Annexin A6 Annexin A7 Annexins Anniversaries and Special Events Annona ...
... orga annexin a5 gene,annexin a5 gene,C1332095,enx2,gngm slc24a3 gene,slc24a3 gene,C1420148,slc24a3,gngm marginal zone of ... golgin a7,gngm trunk of eleventh anterior intercostal vein,trunk of eleventh anterior intercostal vein,C1186581,eleventh ... gngm annexin ii ligand,annexin ii ligand,C1419782,calpactin i, light chain,gngm facet for seventh costal cartilage of sternum, ... golgin a7,gngm cochlear branch of labyrinthine artery,cochlear branch of labyrinthine artery,C0226239,arteria cochlearis ...
... orga annexin a5 gene,annexin a5 gene,C1332095,enx2,gngm slc24a3 gene,slc24a3 gene,C1420148,slc24a3,gngm marginal zone of ... golgin a7,gngm trunk of eleventh anterior intercostal vein,trunk of eleventh anterior intercostal vein,C1186581,eleventh ... gngm annexin ii ligand,annexin ii ligand,C1419782,calpactin i, light chain,gngm facet for seventh costal cartilage of sternum, ... golgin a7,gngm cochlear branch of labyrinthine artery,cochlear branch of labyrinthine artery,C0226239,arteria cochlearis ...
annexin. 19 Select filter option. actin family cytoskeletal protein. 15 Select filter option. cytoskeletal protein. 15 Select ... S100A7L2Protein S100-A7-like 2. help help. Gene Details. Gene Symbol: S100A7L2 ...
annexin. 19 Select filter option. actin family cytoskeletal protein. 15 Select filter option. cytoskeletal protein. 15 Select ... S100A7L2Protein S100-A7-like 2. help help. Gene Details. Gene Symbol: S100A7L2 ...
Human ANXA11(Annexin A11) ELISA Kit. *Human PPARd(Peroxisome Proliferator Activated Receptor Delta) ELISA Kit ... Human S100A7(S100 Calcium Binding Protein A7) ELISA Kit. *Human CDH17(Cadherin 17) ELISA Kit ...
Human ANXA1(Annexin A1) ELISA Kit. * Human ANXA11(Annexin A11) ELISA Kit ... Human S100A7(S100 Calcium Binding Protein A7) ELISA Kit. * Human S100B(S100 Calcium Binding Protein B) ELISA Kit ...
Human ANXA10(Annexin A10) ELISA Kit. *Human ANXA9(Annexin A9) ELISA Kit ... Human RNASE7(Ribonuclease A7) ELISA Kit. *Human RNASE8(Ribonuclease A8) ELISA Kit ...
Human ANXA10(Annexin A10) ELISA Kit. *Human ANXA9(Annexin A9) ELISA Kit ... Human RNASE7(Ribonuclease A7) ELISA Kit. *Human RNASE8(Ribonuclease A8) ELISA Kit ...
  • Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. (wikipedia.org)
  • Description: A Rabbit Polyclonal antibody against Annexin I from Human. (cotinis.com)
  • Description: A Rabbit Polyclonal antibody against Annexin X from Human/Mouse. (cotinis.com)
  • Annexin A4" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • 1. Tissue microarray analysis delineate potential prognostic role of Annexin A7 in prostate cancer progression. (nih.gov)
  • 8. Potential role of annexin A7 in cancers. (nih.gov)