Phospho-IRS-1 (S312) Polyclonal Antibody, 100 µg, (ATB-P0571)

Background: May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).Product datasheet: Overview Product Description Species Reactivities Human,Mouse,Rat Immunogen Synthesized peptide derived from human IRS-1 around the phosphorylation site of S312. Properties Form Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. Storage Instructions-20°C/1 year Clonality Polyclonal References: Human skeletal muscle insulin receptor substrate-1. Characterization of the cDNA, gene, and chromosomal localization. Araki E., Sun X.J., Haag B.L. III, Chuang L.M., Zhang Y., Yang-Feng T.L., White M.F., Kahn C.R.Diabetes 42:1041-1054(1993) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle. Cloning and increased expression of an insulin receptor substrate-1-like gene in human hepatocellular carcinoma. Nishiyama M., Wands J.R.Biochem. Biophys. Res. Commun. 183:280-285(1992) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye. The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitro. Smith L.K., Bradshaw M., Croall D.E., Garner C.W.Biochem. Biophys. Res. Commun. 196:767-772(1993) [PubMed] [Europe PMC] Cited for: TURNOVER. Non-SH2 domains within insulin receptor substrate-1 and SHC mediate their phosphotyrosine-dependent interaction with the NPEY motif of the insulin-like growth factor I receptor. Craparo A., O'Neill T.J., Gustafson T.A.J. Biol. Chem. 270:15639-15643(1995) [PubMed] [Europe PMC] Cited for: INTERACTION WITH IGF1R. Distinct modes of interaction of SHC and insulin receptor substrate-1 with the insulin receptor NPEY region via non-SH2 domains. He W., O'Neill T.J., Gustafson T.A.J. Biol. Chem. 270:23258-23262(1995) [PubMed] [Europe PMC] Cited for: INTERACTION WITH INSR. Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain. Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.Mol. Cell. Biol. 15:2500-2508(1995) [PubMed] [Europe PMC] Cited for: INTERACTION WITH INSR. Adipose-specific expression, phosphorylation of Ser794 in insulin receptor substrate-1, and activation in diabetic animals of salt-inducible kinase-2. Horike N., Takemori H., Katoh Y., Doi J., Min L., Asano T., Sun X.J., Yamamoto H., Kasayama S., Muraoka M., Nonaka Y., Okamoto M.J. Biol. Chem. 278:18440-18447(2003) [PubMed] [Europe PMC] Cited for: MUTAGENESIS OF SER-794, PHOSPHORYLATION AT SER-794. Protein kinase C Theta inhibits insulin signaling by phosphorylating IRS1 at Ser(1101). Li Y., Soos T.J., Li X., Wu J., Degennaro M., Sun X., Littman D.R., Birnbaum M.J., Polakiewicz R.D.J. Biol. Chem. 279:45304-45307(2004) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION AT SER-1101. ALK receptor tyrosine kinase promotes cell growth and neurite outgrowth. Motegi A., Fujimoto J., Kotani M., Sakuraba H., Yamamoto T.J. Cell Sci. 117:3319-3329(2004) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION BY ALK, INTERACTION WITH ALK.