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Description:
MyoGEF functions as a guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. It activates RHOG but not activate RAC1, or to a much lower extent than RHOA and RHOG. Part of a functional unit, involving MyoGEF, MYH10 and RHOA, at the cleavage furrow to advance furrow ingression during cytokinesis. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with EZR, required for normal macropinocytosis.
Description:
Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).
Description:
Required for renal tubular integrity.Tissue specificity: Highest expression in thyroid, adrenal gland and skin. Low levels in spleen, colon and uterus. Overexpressed in breast tumors, with highest expression in infiltrating ductal carcinomas and moderate levels in mucinous adenocarcinoma.
Description:
ERCC6L belongs to the SNF2 ATPase family and acts as an essential component of the spindle assembly checkpoint. It contributes to the mitotic checkpoint by recruiting MAD2 to kinetochores and monitoring tension on centromeric chromatin. It acts as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L may also play a role in the teratogenic action of alcohol.
Description:
Component of the nuclear pore complex that has a direct role in nuclear protein import. Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling. Interacts with multiple transport receptor proteins including CDKN1B. This interaction is required for correct intracellular transport and degradation of CDKN1B.
Description:
The insulin receptor related receptor (IRR) is a heterotetrameric transmembrane receptor composed of two alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. Member of the insulin RTK family, IRR shares high homology with the insulin (IR) and the insulin-like growth factor-1 receptor (IGF-1R), but doesn’t bind any of IR and IGF-1R known ligands. In contrast to the widespread patterns of expression to IR and IGF-1R, IRR demonstrates a very restricted cellular distribution in a subset of tissues of neuronal origin and its biological functions are still unknown.
Description:
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division.
Description:
Lymphotactin is a chemokine-like molecule produced selectively, if not exclusively, by activated CD8+ T cells (1). Lymphotactin is a C-type member of the chemokine superfamily, but retains only the 2nd and 4th of the four cysteine residues conserved in other chemokines (3,4). In normal tissues, lymphotactin is expressed at high levels in spleen, thymus, small intestine, and peripheral blood leukocytes, as well as at low levels in lung, prostate, and ovary (2). Lymphotactin is chemotactic for CD4+ and CD8+ T cells but not for monocytes, and induces a rise in intracellular calcium in peripheral blood lymphocytes (1). The specific receptor for lymphotactin is XCR1, a member of the G protein-coupled receptor family (5). The gene which encodes lymphotactin maps to human chromosome 1q23 (1,2).
Description:
This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.
Description:
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].
Description:
Making up nearly 6% of the human genome, chromosome 6 contains around 1200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf165 gene product has been provisionally designated C6orf165 pending further characterisation.
Description:
Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 induces activation of intracellular Signalling molecules, such as SKY, MAPK1/3 (ERK1/2), MAPK14/P38MAPK and PI3K leading to multifunctional effects, like reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B (By similarity). Positively regulates adipogenesis and adipocyte metabolism.
Description:
The Oxysterol-binding protein (OSBP) family of proteins consist of OSBP (OSBP1) and OSBP2 (ORP-4), which share a high overall similarity. OSBPs are involved in lipid metabolism and signal transduction, as well as vesicle transport, and can translocate to the periphery of Golgi membranes when they are bound to oxysterols. The OSBP protein transports sterols from lysosomes to the nucleus, where sterols downregulate the genes for HMG synthetase, HMG-CoA reductase and the low density lipoprotein receptor (LDLR). OSBP localizes to the cytosol and is widely expressed, while OSBP2 is mainly detected in testis, retina and fetal liver. The extracellular signal-regulated kinase (ERK) signaling pathway is controlled by OSBP via its cholesterol-binding properties. OSBP binds with a high affinity to 25-hydroxy-cholesterol (25-HC), a suppressor of cholesterol synthesis gene transcription in cultured cells.
UOM:
1 * 100 µl
Promotion
,BOSSBS-6560R-CY5.5EA
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