127964 Results for: "Bioss"

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GTPase-activating protein (GAP) promoting GTP hydrolysis on RHOA, CDC42 and RAC1 small GTPases. May be involved in the differentiation of neuronal cells during the formation of neurite extensions. Involved in NMDA receptor activity-dependent actin reorganization in dendritic spines. May mediate cross-talks between Ras- and Rho-regulated signaling pathways in cell growth regulation. Isoform 2 has higher GAP activity (By similarity).

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WFDC5 is a member of the WAP-type four-disulfide core (WFDC) domain family. It is a putative acid-stable proteinase inhibitor.

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Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.

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Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorgenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation.

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Anti-C1orf183 Rabbit Polyclonal Antibody

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RNF113A is a novel gene whose function cannot directly be inferred from it's sequence analysis. Ring finger proteins have a role in signalling the destruction of a range of heterologous protein substrates. They are small zinc binding domains present within arrays of larger, functionally distinct proteins, often close to the amino or carboxyl termini. RNF113A is a ubiquitously expressed protein that contains a RING type zinc finger and a C3H1 type zinc finger.

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Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription.

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DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.

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Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

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COPA (alpha-coat protein) is processed to produce Xenin. Xenin stimulates exocrine pancreatic secretion to affect small and large intestinal motility, and inhibits pentagastrin-stimulated secretion of acid. In the gut, Xenin interacts with the neurotensin receptor. Membrane and vesicular trafficking in the early secretory pathway are mediated by non-Clathrin COP (coat protein) I-coated vesicles. COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, is composed of two subcomplexes. The first consists of the COPB, COPG, COPD and COPZ subunits (also known as b-, g-, d- and z-COP, respectively), which are distantly homologous to AP Clathrin adaptor subunits. The second consists of the COPA, b'-COP and COPE subunits (also known as a-COP, COPP and e-COP, respectively).

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GSTZ1 is a member of the glutathione S transferase (GSTs) super family, encoding multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme also plays a significant role in the catabolism of phenylalanine and tyrosine. Several transcript variants of this gene encode multiple protein isoforms. GSTZ1 shows minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. It has low glutathione peroxidase activity with T butyl and cumene hydroperoxides and is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. Highest expression in liver followed by kidney, skeletal muscle and brain. Also expressed in melanocytes, synovium, placenta, breast and fetal liver and heart.

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Anti-GMEB1 Rabbit Polyclonal Antibody

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GLYATL1 is a 302 amino acid mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL1 can also conjugate a multitude of substrates to form a variety of N-acylglycines. A member of the glycine N-acyltransferase family, GLYATL1 exists as two alternatively spliced isoforms and is encoded by a gene that maps to human chromosome 11q12.1. Chromosome 11 houses over 1,400 genes and comprises nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that maps to chromosome 11.

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GMPPA is a GDP-mannose pyrophosphorylase which catalyzes the conversion of mannose-1-phosphate and GTP to GDP-mannose, in the production of N-linked oligosaccharides.

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HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

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The Tenascin family of extracellular matrix proteins includes Tenascin (also designated cytotactin or Tenascin-C), Tenascin-R (also designated Restrictin or Janusin) and Tenascin-X. Tenascin proteins function as substrate-adhesion molecules (SAMs) and are involved in regulating numerous developmental processes, such as morphogenetic cell migration and organogenesis. The Tenascin family proteins arise from various splicing events in the region of coding for FNIII repeats. Tenascin and Tenascin-X are expressed in several tissues during embryogenesis, and in adult tissues undergoing active remodel-ing such as healing wounds and tumors. Tenascin-R (TN-R) is expressed on the surface of neurons and glial cells.

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FADD (Fas Associated Death Domain) is an apoptosis adapter molecule enabling transduction of the apoptosis signal initiated via the FasL/Fas receptor interaction. The protein contains a C terminal death domain that interacts with the Fas receptor death domain. The N terminus contains a death effectors domain (DED) which recruits caspase to the death inducing signaling complex (DISC) and initiates the apoptotic caspase cascade. Recruitment of Caspase 8 to the Fas receptor results in oligomerization of the Caspase 8 protein, which in turn drives its autoactivation through self-cleavage. Activated Caspase 8 then activates other downstream caspases including Caspase 9, thereby commiting the cell to undergo apoptosis. FADD is implicated in non-apoptotic cellular pathways such as the regulation of cell cycle machinery in T lymphocytes. This is connected to the phosphorylation state of FADD and to the FasL/TRAIL induced transcriptional activation of cfos protooncogene. FADD also interacts with the hepatitis C virus core protein in the HEK 293 cell line.

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Anti-GNG5 Rabbit Polyclonal Antibody

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Anti-GOLGA7 Rabbit Polyclonal Antibody

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Anti-GNPTG Rabbit Polyclonal Antibody

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SPR, also known as sepiapterin reductase, is a homodimeric cytoplasmic protein that belongs to the sepiapterin reductase family. SPR functions as an NADH-dependent aldo-keto reductase and specifically catalyzes the reduction of pteridine derivatives. In addition, SPR plays an important role in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the final reduction step of the synthesis pathway. BH4 is an essential cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine) and is required for proper dopamine synthesis. Mutations in the gene encoding SPR can cause sepiapterin reductase deficiency, a monoamine neurotransmitter deficiency without hyperphenylalaninemia. Sepiapterin reductase deficiency interferes with BH4 synthesis, resulting in DOPA-responsive dystonia and a variety of other human diseases. In addition, SPR mRNA expression is increased in the brain of Parkinson’s Disease (PD) patients, suggesting that SPR may play a role in PD.

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Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.

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Potent vasoconstrictor.

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Cutaneous T cell lymphomas (CTCL) represent a group of malignancies that originate from CD4-T lymphocytes and manifest on the skin. CTCL is a general term for several neoplasms including mycosis fungoides, T cell leukemia/ lymphoma and pagetoid reticulosis, all of which are very difficult to treat in the advanced stages. CTAGE2 (cutaneous T cell lymphoma associated-antigen 2) is a member of the cancer/testis antigen family of proteins (CTAGE) that, under normal conditions, are found primarily in the testis with little or no expression in other parts of the body. Another member of the CTAG family, namely CTAGE5 (also known as MEA11, MEA6, MGEA11 or MGEA6), is a tumor associated antigen that is found in tumors of various origins, including cutaneous T cell lymphomas. Both CTAGE2 and CTAGE5 are expressed as multiple isoforms due to alternative splicing events.

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This gene encodes a member of the family of carcinoembryonic antigen-related cell adhesion molecules (CEACAMs), which are used by several bacterial pathogens to bind and invade host cells. The encoded transmembrane protein directs phagocytosis of several bacterial species that is dependent on the small GTPase Rac. It is thought to serve an important role in controlling human-specific pathogens by the innate immune system. Alternatively spliced transcript variants have been described, but their biological validity has not been determined. [provided by RefSeq, Jul 2008].

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CLUAP1 (Clusterin associated protein 1) is a 413 amino acid nuclear protein that exists as two alternatively spliced isoforms that interact with Clusterin. CLUAP1 is suggested to play a role in apoptosis and cell proliferation, and is expressed in testis, thrachea and thyroid, with low levels found in adrenal gland and spinal cord. The gene encoding CLUAP1 maps to human chromosome 16, which encodes over 900 genes and comprises nearly 3% of the human genome. The GAN gene is located on chromosome 16 and, with mutation, may lead to giant axonal neuropathy, a nervous system disorder characterized by increasing malfunction with growth. The rare disorder Rubinstein-Taybi syndrome is also associated with chromosome 16, as is Crohn's disease, which is a gastrointestinal inflammatory condition.

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May play a negative role in growth factor receptor signaling pathways.

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The exact function of ATXN7L1 remains unknown.

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Progression of cells from interphase to mitosis involves alterations in cell structures and activities. The transition from G2 to M phase is induced by M phase promoting factor, or MPF. In M phase, many proteins are phosphorylated directly by MPF or indirectly by kinases activated by MPF. These M phase phosphoproteins (MPPs, or MPHOSPHs) permit disassembly of interphase structures and generation of M phase enzymatic activities and structures. VAM1 or MPP6 is thought to be a nucleolus specific exosome co factor, required for its role in the maturation of 5.8S rRNA.

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The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.