AMPK Control Cell ExtractsProduct information
|200 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Metabolism
AMPK Control Cell Extracts #9158
|9158S||200 µl (10 western blots)||---||In Stock||---|
Untreated AMPK Control Cell Extracts: Total cell extracts from C2C12 cells, prepared with serum, serve as a negative control.
Treated AMPK Control Cell Extracts: Total cell extracts from C2C12 cells, prepared by serum starvation, serve as a positive control.
As controls, CST recommends using 20 µl of untreated and treated AMPK Control Cell Extract. Boil sample for 3-5 minutes before use.
AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).
- Hardie, D.G. (2004) J Cell Sci 117, 5479-87.
- Carling, D. (2004) Trends Biochem Sci 29, 18-24.
- Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87.
- Lizcano, J.M. et al. (2004) EMBO J 23, 833-43.
- Shaw, R.J. et al. (2004) Proc Natl Acad Sci USA 101, 3329-35.
- Woods, A. et al. (2003) J Biol Chem 278, 28434-42.
- Warden, S.M. et al. (2001) Biochem J 354, 275-83.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
- 2603 AMPKα (23A3) Rabbit mAb
- 2532 AMPKα Antibody
- 4150 AMPKβ1/2 (57C12) Rabbit mAb
- 4148 AMPKβ2 Antibody
- 3662 Acetyl-CoA Carboxylase Antibody
- 7074 Anti-rabbit IgG, HRP-linked Antibody
- 7727 Biotinylated Protein Ladder Detection Pack
- 2535 Phospho-AMPKα (Thr172) (40H9) Rabbit mAb
- 4188 Phospho-AMPKα (Thr172) (D79.5E) Rabbit mAb
- 2531 Phospho-AMPKα (Thr172) Antibody
- 4184 Phospho-AMPKα1 (Ser485) Antibody
- 4185 Phospho-AMPKα1 (Ser485)/AMPKα2 (Ser491) Antibody
- 4181 Phospho-AMPKβ1 (Ser108) Antibody
- 4186 Phospho-AMPKβ1 (Ser182) Antibody
- 3661 Phospho-Acetyl-CoA Carboxylase (Ser79) Antibody
- 6883 SignalFire™ ECL Reagent
- 12757 SignalFire™ Elite ECL Reagent
- 12630 SignalFire™ Plus ECL Reagent
This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.