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| Catalog Code: | NSB804 |
| Product Name: | Insulin Receptor Phosphospecific Antibody |
| Product Description: | Rabbit Polyclonal anti-Insulin Receptor [Tyr1162/Tyr1163] |
| Clonality: | Polyclonal |
| ListPrice: | 325 |
| Immunogen: | Synthetic phosphopeptide derived from the region of Insulin Receptor/IGF1R that contains tyrosines 1162 and 1163. The corresponding residues in the IGF1R are 1135 and 1136. |
| Specificity: | Although exhibiting a preference for IR/IGF-1R, this antibody has been shown by both peptide competition and protein blotting to react with other dual phosphotyrosine motifs from proteins such as c-Met and Shc. |
| Cross Reactivity: | Cross-reacts with Human. Expected to cross-react with Mouse (100% identity with immunogen), Rat (100% identity with immunogen) due to sequence homology. Not yet tested in other species. |
| Packaging: | 0.1 ml Immunogen affinity purified Rabbit antisera. |
| Uses: | This antibody can be used in western blot, where a band of approximately 120 kDa is detected. Previous lots of this antibody have been used in immunostaining. |
| Localization: | Type I membrane protein |
| Background: | Biological actions of Insulin and IGF1 are mediated by their respective cell surface receptor tyrosine kinases that regulate multiple signaling pathways through activation of a series of phosphorylation cascades. The Insulin Receptor and IGF1R are heterotetrameric proteins consisting of two ligand-binding alpha subunits and two beta subunits that each contain a tyrosine kinase domain. Insulin/IGF1 binding to the extracellular domain leads to auto-phosphorylation of the receptor and activation of the intrinsic tyrosine kinase activity, leading to tyrosine phosphorylation of downstream target proteins. These two receptors differ in sequence in regions that confer specificity for the designated ligand as well as in certain intracellular signaling domains, resulting in significant differences in the functional consequences of activation of each receptor. The catalytic loops within the tyrosine kinase domains of the Insulin Receptor/IGF1R contain a three tyrosine motif corresponding to tyrosines 1158, 1162 and 1163 (for the IR) and 1131, 1135 and 1136 (for the IGF1R). It is generally believed that autophosphorylation within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 or 1135), followed by phosphorylation at the first tyrosine (1158 or 1131), then the last (1163 or 1136), upon which the Insulin Receptor or IGF1R becomes fully active. |
| Storage: | Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles. |
| Purity: | Immunogen affinity purified |
| Isotype: | IgG |
| Host Name: | Rabbit |
| Buffer: | Constituents: 50% Glycerol, PBS, 1mg/ml BSA. pH 7.3 |
| Application Summary: | Western Blot: Use at a dilution of 1/1000. |
| Species Summary: | Hu, , |
| Alternate Names: | anti-IGFR1 antibody, anti-Insulin growth factor 1 receptor antibody, anti-CD221 antibody |
| Package Size: | 0.1 ml |
| Preservative: | 0.05% Sodium Azide |
| Homology: | Mouse (100% identity with immunogen), Rat (100% identity with immunogen) |
| Phosphorylated: | Tyr1162/Tyr1163 |
| General References: | 1. Bevan P., Insulin signalling. J Cell Sci 114:1429-30 (2001). 2. Ebina Y., et al. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 40:747-58 (1985). 3. Galic, S., et al. Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP. Mol. Cell. Biol. 23(6): 2096-2108, 2003. 4. Ottensmeyer, F.P., et al. Mechaism of transmembrane signaling: insulin binding and the insulin recpetor. Biochemistry. 39(40):12103-12112, 2000. 5. Ullrich, A., et al. Human insulin recpetor and its relationship to the tyrosine family of oncogenes. Nature. 313(6005):756-761, 1985. |
| Product References: | 1. Wick KR, et al. Grb10 inhibits insulin-stimulated insulin receptor substrate (IRS)-phosphatidylinositol 3-kinase/Akt signaling pathway by disrupting the association of IRS-1/IRS-2 with the insulin receptor. J Biol Chem 278:8460-7, 2003. 2. Pender C., et al. Regulation of insulin receptor function by a small molecule insulin receptor activator. J Biol Chem 277:43565-71, 2002. |
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