AMPKα (D5A2) Rabbit mAb (Biotinylated) #4811

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Supporting Data

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

Application Key:

WB-Western Blotting

Species Cross-Reactivity Key:

H-Human
M-Mouse
R-Rat
Mk-Monkey
B-Bovine

Product Information

Product Description

This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated AMPKα (D5A2) Rabbit mAb #5831.

MW (kDa)

Product Usage Information

Application	Dilution
Western Blotting	1:1000

Storage

Supplied in 136 mM NaCl, 2.6 mM KCI, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibodies.

Protocol

Specificity / Sensitivity

AMPKα (D5A2) Rabbit mAb (Biotinylated) detects endogenous levels of total AMPKα protein.

Species Reactivity:

Human, Mouse, Rat, Monkey, Bovine

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg21 of human AMPKα.

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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For Research Use Only. Not For Use In Diagnostic Procedures.

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