Technical Data
IRS-1 (Insulin Receptor Substrate 1) (Agarose)
Insulin Receptor Substrate (IRS-1) is one of the major substrates of Insulin Receptor Kinase. IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2 domain-containing proteins (Grb2, p85, SHP-2, Fyn and others) and which mediate the metabolic and growth promoting functions of insulin. IRS-1 also contains over 30 potential Ser/Thr phosphorylation sites for kinases, such as PKA, PKC and MAPK. The phosphorylation of Ser 612 and Ser636/639 are mediated by PKA and mTOR pathways, respectively, resulting in an inhibition of insulin signaling in the cell and suggesting a potential mechanism for insulin resistance in some models of obesity. Once phosphorylated by insulin receptor, IRS-1 recruits the downstream components that mediate the insulin signaling. IRS-1 protein contains a conserved pleckstrin homology (PH) domain located at its amino terminus, adjacent to a phospho-tyrosine binding (PTB) domain.

Immunoprecipitation: 50ul immunoprecipitates IRS-1 from 500ug of a RIPA lysate of 3T3/A31 mouse fibroblasts. After boiling in SDS-PAGE sample buffer a small amount of the non-covalently bound IgG light chain (28kDa) and heavy chain (55kDa) may be observed.

Elution Buffer % IRS-1 Released SDS-Page sample buffer 100 0.5M Glycine, pH 2, 0 0.1M TEA, pH 11.5.

Affinity Purification: The antibody-agarose may be useful for affinity purification of proteins that bind IRS-1.
PabIgGAffinity Purified
200ug-20CBlue IceRatRabbit
Carboxy-terminal 14 amino acid peptide of rat liver IRS-1 (CYASINFQKQPEDRQ).
Purified by affinity chromatography.
Provided as a 50% gel slurry in PBS, 0.05% azide.
Recognizes rat IRS-1.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.