IRS1
Reactivity: Human
WB, IHC, ELISA, IF
Host: Rabbit
Polyclonal
unconjugated
Sample Volume
20 μL
Restrictions
For Research Use only
Format
Liquid
Buffer
Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C
Storage Comment
The antibody was conjugated with R-PE under optimum conditions, and unconjugated antibody and free PE were removed. Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.
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).
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).
Burks, White: "IRS proteins and beta-cell function." in: Diabetes, Vol. 50 Suppl 1, pp. S140-5, (2001) (PubMed).
Paz, Liu, Shorer, Hemi, LeRoith, Quan, Kanety, Seger, Zick: "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).
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.