Product Pathways - Metabolism
Phospho-AS160 (Thr642) Antibody #4288
|4288S||100 µl (10 western blots)||---||In Stock||---|
|4288||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Mouse, Rat.
Specificity / Sensitivity
Phospho-AS160 (Thr642) Antibody detects endogenous levels of AS160 protein only when phosphorylated at Thr642.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence around Thr642 of human AS160. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from serum starved HeLa cells, untreated or treated with either insulin (150 nM, 15 minutes) or IGF-1 #3093 (100 ng/ml, 15 minutes), using Phospho-AS160 (Thr642) Antibody (upper) or AS160 (C69A7) Rabbit mAb #2670 (lower). The phospho-specificity of the antibody is verified by λ-phosphatase treatment of the above cell lysates.
Insulin is a major hormone controlling critical energy functions, such as glucose and lipid metabolism. Insulin binds to and activates the insulin receptor (IR) tyrosine kinase, which phosphorylates and recruits adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of the Glut4 glucose transporter from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt Ser/Thr kinase (AS160, TBC1D4) is a Rab GTPase-activating protein that regulates insulin-stimulated Glut4 trafficking. AS160 is expressed in many tissues including brain, kidney, liver, and brown and white fat (2). Multiple Akt phosphorylation sites have been identified on AS160 in vivo, with five sites (Ser318, Ser570, Ser588, Thr642, and Thr751) showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrate that insulin-stimulated phosphorylation of AS160 is a crucial step in Glut4 translocation (3) and is reduced in some patients with type 2 diabetes (4). The interaction of 14-3-3 regulatory proteins with AS160 phosphorylated at Thr642 is a necessary step for Glut4 translocation (5). Phosphorylation of AS160 by AMPK is involved in the regulation of contraction-stimulated Glut4 translocation (6).
- Watson, R.T. and Pessin, J.E. (2006) Trends Biochem. Sci. 31, 215-222.
- Kane, S. et al. (2002) J. Biol. Chem. 277, 22115-22118.
- Sano, H. et al. (2003) J. Biol. Chem. 278, 14599-14602.
- Karlsson, H.K. et al. (2005) Diabetes 54, 1692-1697.
- Ramm, G. et al. (2006) J. Biol. Chem. 281, 29174-29180.
- Kramer, H.F. et al. (2006) J. Biol. Chem. 281, 31478-31485.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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