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Insulin Receptor Substrate 1 (IRS1) (pTyr896) antibody

Details for Product No. ABIN967601, Supplier: Log in to see
Antigen
  • irs1
  • irsu
  • IRS1
  • HIRS-1
  • G972R
  • IRS-1
  • IRS1IRM
  • irs-1
  • irs1-a
Alternatives
anti-Human Insulin Receptor Substrate 1 antibody for Enzyme Immunoassay
Epitope
pTyr896
55
49
44
44
24
22
21
21
16
16
15
14
13
13
13
13
13
13
9
9
8
7
6
5
5
4
4
4
4
4
3
3
3
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
513
354
337
11
9
5
1
1
Host
Mouse
511
29
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
13
12
11
11
11
10
10
10
10
10
10
10
2
1
1
1
Application
Western Blotting (WB)
312
215
137
112
102
79
30
30
12
4
2
1
Supplier
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Brand BD Pharmingen™
Immunogen Phosphorylated Human IRS-1 Peptide
Clone K9-211
Isotype IgG2a, kappa
Characteristics 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.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name IRS-1 (IRS1 Antibody Abstract)
Background 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.
Molecular Weight 160-185 kDa
Pathways Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway
Comment

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer Aqueous buffered solution containing ≤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 Store undiluted at 4°C.
Supplier Images
Western Blotting (WB) image for anti-Insulin Receptor Substrate 1 (IRS1) (pTyr896) antibody (ABIN967601) Western blot analysis of IRS-1 (pY896) in transformed human epithelial cells. Lysates...
Product cited in: 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 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).

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).

Background publications 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).