anti-IRS4, pAb

CHF 315.00
In stock
YIF-LF-PA0085100 µlCHF 315.00
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Product Details
Synonyms IRS4; py160; IRS-4; pp160; Phosphoprotein of 160 kDa; Insulin Receptor Substrate 4; 160 kDa Phosphotyrosine Protein
Product Type Polyclonal Antibody
Immunogen/Antigen Synthetic peptide.

Western Blot (1:2,000)

Crossreactivity Human
Purity Detail Protein A purified.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Rabbit IgG

Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
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Product Specification Sheet
Datasheet Download PDF

Insulin receptor substrate (IRS) proteins play a central role in maintaining basic cellular functions such as growth and metabolism through insulin/insulin like growth factor (IGF) signaling. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified which differ in their subcellular distribution and interaction with SH2 domain proteins. After phosphorylation by activated receptors, these intracellular signaling molecules recruit various downstream effector pathways including phosphatidylinositol 3-kinase, tyrosine protein phosphatase SHPTP-2, and several smaller adapter molecules such as the growth factor receptor-binding protein Grb-2. IRS-1, the best characterized IRS protein, has eighteen potential tyrosine phosphorylation sites which directly bind to SH2 domains in downstrem proteins. IRS-1 consists of amino terminal containing pleckstrin homology (PH) domain followed by a phosphotyrosine-binding (PTB) domain which binds to IR and IGFR, and carboxy terminal containing multiple tyrosine and serine residues which become docking sites for proteins that have PTB domain such as SH2 domain. IRS-4 is the last identified member of the IRS family. Cloning of human IRS-4 revealed a predicted protein of similar length to both IRS-1 and IRS-2and showed only 27% and 29% identity with IRS-1 and IRS-2, respectively. In contrast, IRS-4 exhibits higher degree of homology in the PH domain (43 to 50 %) and the PTB domain (43 to 66%) with the corresponding domains in IRS-1, IRS-2 and IRS-3. IRSs are also thought to be able to induce malignant transformation. IRS-1 has been shown to be constitutively active in breast cancer. Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May acts as negative regulators of the IGFI signaling pathway by suppressing the function of IRS1 and IRS2.

Product References

1) Dearth R.K. et al., (2007) Cell Cycle. 6:705-713. (General)
2) White M.F., (2002) Am J Physiol Endocrinol Metab. 283:E413-E422. (General)
3) Burks D.J. and White M.F., (2001) Diabetes 50:S140-S145. (General)
4) Giovannone B. et al., (2000) Diabetes Metab Res Rev. 16:434-441. (General)

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