Product Pathways - Glucose Metabolism
AS160 Antibody #2447
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H | Endogenous | 160 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
AS160 Antibody detects endogenous levels of total AS160 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) derived from the sequence around Gly1286 of human AS160. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from HepG2 and 293 cells using AS160 Antibody.
Background
The polypeptide 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 different adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of GLUT4 glucose transporters from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt serine/threonine 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 were identified on AS160 in vivo, with five sites showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrated 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 another 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.
Application References
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.
