A phospho specific peptide corresponding to residues surrounding Tyrosine 632 of human IRS-1 was used as an immunogen. This antibody only detects IRS-1 phosphorylated at Tyrosine 632.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Insulin receptor substrates (IRS), the major intracellular substrates of the insulin receptor (IR), are adaptor proteins that transduce signals from the IR to downstream effectors that are important for the biological effect of insulin (1, 2). After insulin stimulation, IRS proteins are rapidly phosphorylated on multiple tyrosine residues. Once phosphorylated, IRS proteins bind and activate Grb-2, SHP2 and the PI3-K p85 subunit (2, 3). IRS-1 functions as one of the key regulators of IR and the insulin-like growth factor-1 receptor. Disruption of IRS-1 causes growth retardation and insulin resistance associated with hypertension, hypertriglyceridemia, and impaired endothelium-dependent vascular relaxation (4, 5).
Related Pathway
Adipogenesis
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