|Other Names||Hepatocyte growth factor-regulated tyrosine kinase substrate, Hrs, Protein pp110, HGS, HRS|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2161c was selected from the Center region of human IMOS-1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down- regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.|
|Cellular Location||Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Endosome, multivesicular body membrane; Peripheral membrane protein|
|Tissue Location||Ubiquitous expression in adult and fetal tissues with higher expression in testis and peripheral blood leukocytes.|
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Ubiquitin is a 76 amino acid highly conserved eukaryotic polypeptide that selectively marks cellular proteins for proteolytic degradation by the 26S proteasome. The process of target selection, covalent attachment and shuttle to the 26S proteasome is a vital means of regulating the concentrations of key regulatory proteins in the cell by limiting their lifespans. Polyubiquitination is a common feature of this modification. Serial steps for modification include the activation of ubiquitin, an ATP-dependent formation of a thioester bond between ubiquitin and the enzyme E1, transfer by transacylation of ubiquitin from E1 to the ubiquitin conjugating enzyme E2, and covalent linkage to the target protein directly by E2 or via E3 ligase enzyme. Deubiquitination enzymes also exist to reverse the marking of protein substrates. Posttranslational tagging by Ub is involved in a multitude of cellular processes, including the cell cycle, cell growth and differentiation, embryogenesis, apoptosis, signal transduction, DNA repair, regulation of transcription and DNA replication, transmembrane transport, stress responses, the immune response, and nervous system functions.
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