Product Pathways - Metabolism
Phospho-IGF-I Receptor β (Tyr1135) (DA7A8) Rabbit mAb #3918
|3918S||100 µl (10 western blots)||---||In Stock||---|
|3918||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat||Endogenous||95||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-IGF-I Receptor β (Tyr1135) (DA7A8) Rabbit mAb detects endogenous levels of IGF-I receptor only when phosphorylated at Tyr1135. This antibody cross-reacts with Tyr1150 of insulin receptor and may also cross-react with other overexpressed related tyrosine-phosphorylated tyrosine kinases.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1135 of human IGF-I receptor β.
Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).
- Adams, T.E. et al. (2000) Cell. Mol. Life Sci. 57, 1050-1093.
- Baserga, R. et al. (2000) Oncogene 19, 5574-5581.
- Scheidegger, K.J. et al. (2000) J. Biol. Chem. 275, 38921-38928.
- Hernandez-Sanchez, C. et al. (1995) J. Biol. Chem. 270, 29176-29181.
- Lopaczynski, W. et al. (2000) Biochem. Biophys. Res. Commun. 279, 955-960.
- Baserga, R. et al. (1999) Exp. Cell Res. 253, 1-6.
- White, M.F. et al. (1985) J. Biol. Chem. 260, 9470-9478.
- White, M.F. et al. (1988) J. Biol. Chem. 263, 2969-2980.
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