Phospho-IRS-1 (S639) Polyclonal Antibody, 100 µg, (ATB-P0149)

Description

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:

References:

1. 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.
2. 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].
3. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
4. 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.
5. 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.
6. 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.
7. 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.
8. 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.
9. 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.
10. 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.