Purified from rabbit serum by sequential epitope-specific chromatography, this product contains enough material for 10 mini-blots. This antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated insulin receptor substrate-1 (IRS-1). The final product is generated by affinity chromatography using IRS-1 derived peptide that is phosphorylated at serine 616.
The antibody has been used in western blotting. Previous lots of this antibody have been used in immunohistochemistry. In western analysis the positive control used was human embryonic kidney cell line transfected with a vector encoding IRS-1 (293T) and stimulated with a phorbol ester, TPA.
IRS-1, a major substrate of the insulin receptor, is phosphorylated in response to stimulation of cells by insulin, insulin-like growth factor 1 (IGF-1) and interleukin 4 (IL-4). IRS-1 is phosphorylated on serine, threonine and tyrosine residues in a variety of tissues. An insulin-sensitive serine/threonine kinase casein kinase II mediates a portion of the insulin-stimulated serine/threonine phosphorylation of overexpressed IRS-1 in vivo. Thr 502 is identified as the major casein kinase II-catalyzed phosphorylation site in rat IRS-1, and Ser 99 is an additional phosphorylation site catalyzed by casein kinase II. Thus, casein kinase II-catalyzed phosphorylation of IRS-1 may be a component of the intracellular insulin signaling cascade. IRS-1 contains three putative binding sites for 14-3-3 (Ser 270, Ser 374 and Ser 641) and the motif around Ser 270 is located in the phosphortyrosine binding domain of IRS-1, which is responsible for the interaction with the insulin receptor.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Insulin receptor substrate 1; IRS-1; pp185
Gene Aliases: G972R; HIRS-1; IRS-1; IRS1; IRS1IRM