Synthetic phosphopeptide derived from human IRS-1 around the phosphorylation site of Serine 307.
Conjugation:
Unconjugated
Alternative Names:
Insulin receptor substrate 1, IRS-1, IRS1
Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase. IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin. IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK and IKK while Ser789 is phosphorylated by SIK-2, a member of the AMPK family. The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively. Phosphorylation of IRS-1 at Ser1101 is mediated by PKCtheta and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2.
Application Dilute:
WB: 1:1000~1:2000
Application Notes:
IRS-1 (Phospho-Ser307) polyclonal antibody detects endogenous levels of IRS-1 protein only when phosphorylated at Ser307.
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