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Description:
Insulin receptor substrates (IRS) are responsible for several insulin related activities, such as glucose homeostasis, cell growth, cell transformation, apoptosis and insulin signal transduction. Serine/threonine phosphorylation of IRS1 has been demonstrated to be a negative regulator of insulin signaling and is responsible for its degradation, although IRS1 degradation pathways are not well understood. IRS1 has also been shown to be constitutively activated in cancers such as breast cancer, Wilm's tumors, and adrenal cortical carcinomas, thus making IRS1 phosphorylation and subsequent degradation an attractive therapeutic target. To date there have been four subtypes identified: IRS1, 2, 3 and 4, with IRS1 being widely expressed.
Description:
IRGM belongs to a family of interferon-gamma inducible GTPases, belonging to the GTPase superfamily, and are selectively induced by IFN-gamma or bacterial lipopolysaccharide (LPS) stimulation. IRGM is primarily expressed in all cells derived from B-cell lineages, and is highly expressed in macrophages following IFN-gamma stimulation. IRGM has been shown to be required for host defences against a broad range of intracellular pathogens. Specifically, IRGM deficient mice show defects with intracellular microbial killing, phagosome maturation and autophagy. More recently IRGM has been shown to inhibit baseline hematopoietic proliferation and is required for a normal hematopoietic stem cell response to chemical and infectious stimuli.
Description:
Velis are a family of small synaptic proteins that interact with other proteins at the post-synaptic density (PSD) of neuronal synapses. Velis contain the PDZ motif involved in recruiting cell adhesion molecules, receptors, and channels. Veli1 (also designated Lin-7A and MALS-1), Veli2 (also designated Lin-7B and MALS-2), and Veli3 (also designated Lin-7C and MALS-3) are mammalian homologs of C. elegans LIN-7. Veli proteins are ubiquitously expressed with high expression in brain, liver, and testis. Velis are localized at the synaptic junctions in neurons. Velis bind to CASK, a neurexin-binding protein highly concentrated in synapses, and Mint1, a binding partner with a vesicle trafficking protein.
Description:
DCAKD belongs to the coaE family. It contains one DPCK (dephospho CoA kinase) domain. There are two isoforms.Coenzyme A (CoA) is an essential cofactor used in numerous biochemical pathways. It plays a critical role in the synthesis and oxidation of fatty acids and is vital to the citric acid cycle. The biosynthesis pathway of CoA from pantothenic acid (also known as vitamin B5) is essential and universal in prokaryotes and eukaryotes. In humans, the final steps of the biosynthesis pathway are carried out by the bifunctional enzyme COASY. The sequence of these enzymes are highly conserved between different bacterial species. The phosphopantetheine adenylyltransferase and decoenzyme A kinase activities of COASY are evolutionarily conserved activities. DCAKD (deCoA kinase domain containing protein) is a 231 amino acid protein that consists of a deCoA kinase domain and an ATP nucleotide binding motif. Localising to mitochondria and the cytosol, DCAKD belongs to the coaE family which suggests that it may play a role in the biosynthesis of CoA.
Description:
DCAKD belongs to the coaE family. It contains one DPCK (dephospho CoA kinase) domain. There are two isoforms.Coenzyme A (CoA) is an essential cofactor used in numerous biochemical pathways. It plays a critical role in the synthesis and oxidation of fatty acids and is vital to the citric acid cycle. The biosynthesis pathway of CoA from pantothenic acid (also known as vitamin B5) is essential and universal in prokaryotes and eukaryotes. In humans, the final steps of the biosynthesis pathway are carried out by the bifunctional enzyme COASY. The sequence of these enzymes are highly conserved between different bacterial species. The phosphopantetheine adenylyltransferase and decoenzyme A kinase activities of COASY are evolutionarily conserved activities. DCAKD (deCoA kinase domain containing protein) is a 231 amino acid protein that consists of a deCoA kinase domain and an ATP nucleotide binding motif. Localizing to mitochondria and the cytosol, DCAKD belongs to the coaE family which suggests that it may play a role in the biosynthesis of CoA.
Description:
May function as a complex with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 which is produced in acute myeloid leukemia with the chromosomal translocation t(8;21). May thus be involved in the repression of AML1-dependent transcription and the induction of G-CSF/CSF3-dependent cell growth. May be a tumor suppressor gene candidate involved in myeloid tumors with the deletion of the 20q11 region.Tissue specificity:Ubiquitously expressed in fetal and adult tissues. Highly expressed in adult brain, heart, lung, kidney, lymph node, appendix, thymus, testis, uterus, small intestine, prostate and thymus.
Description:
Velis are a family of small synaptic proteins that interact with other proteins at the post-synaptic density (PSD) of neuronal synapses. Velis contain the PDZ motif involved in recruiting cell adhesion molecules, receptors, and channels. Veli1 (also designated Lin-7A and MALS-1), Veli2 (also designated Lin-7B and MALS-2), and Veli3 (also designated Lin-7C and MALS-3) are mammalian homologs of C. elegans LIN-7. Veli proteins are ubiquitously expressed with high expression in brain, liver, and testis. Velis are localized at the synaptic junctions in neurons. Velis bind to CASK, a neurexin-binding protein highly concentrated in synapses, and Mint1, a binding partner with a vesicle trafficking protein.
Description:
Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7).
UOM:
1 * 100 µl
Promotion
,BOSSBS-1610R-FITCEA
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