AMPK is a heterotrimeric complex comprising a catalytic alpha subunit and regulatory beta and gamma subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase, and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxymethylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKalpha1 and AMPKalpha2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKbeta1 encodes a 271 amino acid protein and human AMPKbeta2 encodes a 272 amino acid protein. The human AMPKgamma1 gene encodes a 331 amino acid protein. Human AMPKgamma2 and AMPKgamma3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-AMPKalpha1 (S486) polyclonal antibody detects endogenous levels of AMPKalpha1 protein only when phosphorylated at Ser486. The antibody does not cross-react with phosphorylated AMPKalpha2 or other related proteins.
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