Technical Data
IRS-1, phosphorylated (Ser307) (Insulin Receptor Substrate 1)
Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain-containing proteins, which mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6). The phosphorylation of Ser612 and Ser636/639 are mediated by the PKC and mTOR pathways, respectively (7,8), resulting in an inhibition of insulin signaling in the cell and suggesting a potential mechanism for insulin resistance in some models of obesity.

Suitable for use in Western Blot and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1,000

Immunoprecipitation: 1:50

Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
100ul4C (-20C Glycerol)Blue IceMouseRabbit
Not determined
Synthetic phosphopeptide corresponding to residues surrounding Ser307 of mouse IRS-1 (KLH coupled). Equivalent to human Ser312.
Purified by Protein A and peptide affinity chromatography.
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Detects overexpressed or endogeneous mouse IRS-1 only when phosphorylated at Ser307 (Mr 175kD). Does not crossreact with other related phospho-proteins. Species Crossreactivity: Predicted to crossreact with human based on sequence homology.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Sun, X.J., et al., 1991, Nature 352: 73-77. 2. Sun, X.J., et al., 1992, J. Biol. Chem. 267: 22,662-22,672. 3. Myers, Jr., M.G., et al., 1993 Endocrinology 132: 1,421-1,430. 4. Wang, L.M., et al., 1993, Science 261: 1,591-1,594. 5. Rui, L., et al., 1997, J. Clin. Invest. 107: 181-189. 6. Gao, Z., et al., 2002, J. Biol. Chem. 277: 48,115-48,121. 7. De Fea, K. and Roth, R.A., 1997, Biochemistry 36: 12,939-12,947. 8. Ozes, O.N., et al., 2001, Proc. Natl. Acad. Sci. USA 98: 4,640-4,645.