Product Pathways - Metabolism
Phospho-AMPKα (Thr172) (D79.5E) Rabbit mAb #4188
|4188L||300 µl (60 western blots)||---||In Stock||---|
|4188S||100 µl (20 western blots)||---||In Stock||---|
|4188||carrier free and custom formulation / quantity||email request|
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|W||1:2000||Human, Mouse, Rat, D. melanogaster, S. cerevisiae||Endogenous||62||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Bovine.
Specificity / Sensitivity
Phospho-AMPKα (Thr172) (D79.5E) Rabbit mAb detects endogenous AMPK-alpha only when phosphorylated at Thr172. This antibody detects both α1 and α2 isoforms of the catalytic subunit, but does not detect the regulatory β or γ subunits.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr172 of human AMPKα.
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.
- Ferla, R. et al. (2012) Oncol Lett 4, 1077-1081. Applications: Western Blotting.
- Otvos, L. et al. (2011) BMC Biotechnol 11, 90. Applications: Western Blotting.
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