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Description:
ATG16 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG16, another member of the autophagy protein family, forms a complex with the ATG5-ATG12 conjugate. This multimeric protein has been shown to be essential for autophagosome formation in both yeast and mammals and targets the ATG5-ATG12 complex to the autophagic isolation membrane during the formation of the autophagosome. Because mammalian ATG16 has seven WD-repeats in its C-terminal domain, it has been suggested that these may form a platform for further protein-protein interactions. Multiple isoforms of ATG16 are known to exist.
Description:
Slitrk1 Antibody: SLIT and NTRK-like family 1 (Slitrk1) is a member a protein family consisting of six homologous transmembrane proteins (Slitrk1-6) that share two conserved leucine-rich repeat domains in the extracellular domain and have significant homology to Slit, a secreted axonal growth-controlling protein. These proteins are also homologous to trk neurotrophin receptors in their intracellular domains. Expression of Slitrk proteins is highly restricted to neural and brain tumor tissues, but varies within the family. For example, Slitrk1 is expressed primarily in mature neurons. Overexpression of Slitrk1 in transfected neuronal cells induced unipolar neurites, while expression of the other Slitrk proteins inhibited neurite outgrowth, suggesting that these proteins are involved in the control of neurite outgrowth. While Slitrk1 variants have been suggested associated with Tourette's Syndrome, it is thought to play only a minor role if at all.
Description:
CXCR4-Lo Antibody: Human immunodeficiency virus (HIV) and related viruses require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b and CCR8 in the chemokine receptor family, and four new human molecules GPR15, STRL33, GPR1 and V28 were recently identified as HIV coreceptors. Among them, CXCR4 is a principal coreceptor for T-cell tropic strains of HIV-1 fusion and entry of human white blood cells. CXCR4 is also required for the infection by dual-tropic strains of HIV-1 and mediates CD-4 independent infection by HIV-2. The alpha-chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1. CXCR4 associates with the surface CD4-gp120 complex before HIV enters target cells. CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells. The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV binding sites.
Description:
LGI3 Antibody: The leucine-rich, glioma inactivated gene 3 (LGI3) is a member of the LGI family in which LGI1 is the exemplar. The LGI family consists of four of highly related proteins containing leucine-rich repeats (LRRs) which are highly similar to other transmembrane signaling molecules and receptors. LGI1 has been identified as a candidate tumor suppressor gene for glioma and plays a role in autodominant lateral temporal epilepsy (ADTLE), an epileptic syndrome characterized by focal seizures with predominant auditory symptoms. Despite its high homology with LGI1 and similar pattern of expression, mutations in LGI3 have not been found to be associated with ADTLE. LGI3 expression is induced in rat astrocyte cultures by the amyloid beta (Abeta) peptide and accumulated on neuronal plasma membranes of aged monkey brains and co-localized with Abeta.
Description:
Slitrk4 Antibody: SLIT and NTRK-like family 4 (Slitrk4) is a member a protein family consisting of six homologous transmembrane proteins (Slitrk1-6) that share two conserved leucine-rich repeat domains in the extracellular domain and have significant homology to Slit, a secreted axonal growth-controlling protein. These proteins are also homologous to trk neurotrophin receptors in their intracellular domains. Expression of Slitrk proteins is highly restricted to neural and brain tumor tissues, but varies within the protein family. Like every other Slitrk protein except Slitrk1, overexpression of Slitrk4 inhibited neurite outgrowth in cultured neurons, suggesting that these proteins are involved in the control of neurite outgrowth.
Description:
Copper amine oxidases catalyze the oxidative conversion of amines to aldehydes and ammonia in the presence of copper and quinone cofactor. The protein contains several conserved motifs including the active site of amine oxidases and the histidine residues that likely bind copper. It may be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine. Copper amine oxidases catalyze the oxidative conversion of amines to aldehydes and ammonia in the presence of copper and quinone cofactor. This gene shows high sequence similarity to copper amine oxidases from various species ranging from bacteria to mammals. The protein contains several conserved motifs including the active site of amine oxidases and the histidine residues that likely bind copper. It may be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine. This gene may be a candidate gene for hereditary ocular diseases. Alternate splicing results in multiple transcript variants.
Description:
Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The enzyme is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This enzyme is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits; this gene encodes the catalytic subunit. Mutations in this gene can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Description:
CYP11A1 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. CYP11A1 localizes to the mitochondrial inner membrane and catalyzes the conversion of cholesterol to pregnenolone, the first and rate-limiting step in the synthesis of the steroid hormones. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane and catalyzes the conversion of cholesterol to pregnenolone, the first and rate-limiting step in the synthesis of the steroid hormones. Two transcript variants encoding different isoforms have been found for this gene. The cellular location of the smaller isoform is unclear since it lacks the mitochondrial-targeting transit peptide.
Description:
SYNPO2 Antibody: SYNPO2 was initially identified as myopodin, a member of the synaptopodin family that contains one PPXY motif and multiple PXXP motifs. It colocalizes with alpha-actinin and is found at the Z-disc and during stress conditions will translocate to the nucleus, suggesting that it is part of signaling pathways in addition to its function as a structural protein. SYNPO2 has been shown to bind to calmodulin, alpha-actinin, and smooth muscle myosin and will stimulate actin polymerization in a calmodulin dependent manner, consistent with its proposed role in organizing the cytoskeleton. While deletion of SYNPO2 has been reported to be highly correlated with the invasiveness of prostate cancers, other reports suggest that down-regulation of SYNPO2 reduces the invasiveness and motility of prostate cancer cells.
Description:
UHRF1BP1 peptide is used for blocking the activity of UHRF1BP1 antibody.
UOM:
1 * 50 µG
Promotion
,PRSI6459PEA
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