Phospho-AMPKα (Thr172) (D4D6D) Rabbit mAb #50081

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Supporting Data

REACTIVITY	H M R
SENSITIVITY	Endogenous
MW (kDa)	62
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
IP-Immunoprecipitation
IHC-Immunohistochemistry

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat

Product Information

Product Usage Information

Application	Dilution
Western Blotting	1:1000
Simple Western™	1:10 - 1:50
Immunoprecipitation	1:50
Immunohistochemistry (Paraffin)	1:200 - 1:800

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Phospho-AMPKα (Thr172) (D4D6D) Rabbit mAb detects endogenous AMPKα only when phosphorylated at threonine 172. The antibody detects both α1 and α2 isoforms of the catalytic subunit, but does not detect the regulatory β or γ subunits.

Species Reactivity:

Human, Mouse, Rat

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Chicken, Zebrafish, Bovine, Pig

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr172 of human AMPKα protein.

Background

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 AMPK activation, 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).

Database Links

UniProt ID: Q13131 , P54646

Entrez-Gene Id: 5562 , 5563

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