Upstream / Downstream

Explore pathways related to this product.

Antibody Guarantee

CST Antibody Performance Guarantee

LEARN MORE  

Questions?

Find answers on our FAQs page.

ANSWERS  

Visit PhosphoSitePlus®

PTM information and tools available.

LEARN MORE

Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-AMPKα (Thr172) (40H9) Rabbit mAb 2535 1 x 100 µl
H M R Hm Mk Dm Sc 62 Rabbit 
AMPKα (D63G4) Rabbit mAb 5832 1 x 100 µl
H M R Mk B 62 Rabbit 

Product Description

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.


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).


1.  Carling, D. (2004) Trends Biochem Sci 29, 18-24.

2.  Hawley, S.A. et al. (1996) J Biol Chem 271, 27879-87.

3.  Lizcano, J.M. et al. (2004) EMBO J 23, 833-43.

4.  Hardie, D.G. (2004) J Cell Sci 117, 5479-87.

5.  Shaw, R.J. et al. (2004) Proc Natl Acad Sci USA 101, 3329-35.

6.  Woods, A. et al. (2003) J Biol Chem 278, 28434-42.

7.  Warden, S.M. et al. (2001) Biochem J 354, 275-83.


Entrez-Gene Id 5562, 5563
Swiss-Prot Acc. Q13131, P54646


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
PhosphoPlus® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.