Insulin Receptor Substrate 1 (IRS1) (pTyr896) antibody
|Synonyms||HIRS-1, G972R, IRS-1, IRS1IRM, irs1, MGC75645, IRS1|
Alternatives Western Blotting (WB)
|6 references available|
|Quantity||0.1 mg (0.5 mg/ml)|
|Price||Product not available in this region.|
|Immunogen||Phosphorylated Human IRS-1 Peptide|
The IRS (Insulin Receptor Substrate) proteins IRS-1, IRS-2, IRS-3, and IRS-4 are major substrates of the insulin receptor and the insulin-like growth factor-1 (IGF-1) receptor tyrosine kinases. IRS proteins contain an N-terminal pleckstrin homology (PH) domain, a phosphotyrosine-binding (PTB) domain, and multiple tyrosine phosphorylation sites in the C-terminus. The IRS-1 protein is widely expressed and, along with IRS-2, mediates somatic growth and carbohydrate metabolic responses to insulin. Following insulin receptor ligation, IRS-1 binds to the juxtamembrane region of the receptor via the PH and PTB domains and is tyrosine phosphorylated, which facilitates its interaction with SH2 domain-containing signaling proteins. Specifically, the phosphorylated tyrosine 896 (pY896) of human IRS-1 is a major binding site for the GRB2 (Growth-factor Receptor-Bound protein 2) adaptor protein. After IRS-1 activation, negative and positive feedback regulates dephosphorylation of its tyrosine sites, which ultimately regulates the magnitude and/or duration of the downstream pleiotropic responses to insulin and IGF-1.
The K9-211 monoclonal antibody recognizes pY896 of human IRS-1. The orthologous phosphorylation sites of mouse and rat IRS-1 are Y891 and Y895, respectively.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
|Molecular Weight||160-185 kDa|
Related Products: ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at 4°C.|
|Restrictions||For Research Use only|
Burks, Bezerra, Le et al.: "Plant initiation factor 3 subunit composition resembles mammalian initiation factor 3 and has a novel subunit." in: The Journal of biological chemistry, Vol. 276, Issue 3, pp. 2122-31, 2001 (PubMed).
Ward, Gough, Rashke et al.: "Systematic mapping of potential binding sites for Shc and Grb2 SH2 domains on insulin receptor substrate-1 and the receptors for insulin, epidermal growth factor, platelet-derived growth factor, and fibroblast growth factor." in: The Journal of biological chemistry, Vol. 271, Issue 10, pp. 5603-9, 1996 (PubMed).
Paz, Liu, Shorer et al.: "Phosphorylation of insulin receptor substrate-1 (IRS-1) by protein kinase B positively regulates IRS-1 function." in: The Journal of biological chemistry, Vol. 274, Issue 40, pp. 28816-22, 1999 (PubMed).
Burks, White: "IRS proteins and beta-cell function." in: Diabetes, Vol. 50 Suppl 1, pp. S140-5, 2001 (PubMed).
White: "IRS proteins and the common path to diabetes." in: American journal of physiology. Endocrinology and metabolism, Vol. 283, Issue 3, pp. E413-22, 2002 (PubMed).
Gual, Le Marchand-Brustel, Tanti: "Positive and negative regulation of insulin signaling through IRS-1 phosphorylation." in: Biochimie, Vol. 87, Issue 1, pp. 99-109, 2005 (PubMed).