Phospho-IRS-1 (Ser789) Antibody

INQUIRY

CAT. NO.: AMA-0013

Target Information
UniProt ID	P35568

Product Details
Size	100 μL
Reactivity	Rat
Storage	Store at -20°C.
Purification	Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser789 of mouse IRS-1 (equivalent to Ser794 of human IRS-1). Antibodies are purified by protein A and peptide affinity chromatography.

Usage
Application	WB
Product Usage Information Dilution	Western Blotting (1:1000)
MW (Target)	180 kDa

Background
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 PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity.

Background

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 PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity.

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