Anti-AMPKα antibody produced in rabbit

AMP-activated protein kinase (AMPK) is an enzyme that regulates responses to hypoxia, increased ATP consumption, heat shock, and nutrient deprivation. This enzyme is a heterotrimer that consists of a catalytic α subunit and two non-catalytic subunits; β and γ. AMPKα regulates the circadian rhythm in fat tissues . Anti-AMPKα detects AMPKα (60 kDa) by immunoblotting. Staining of the AMPKα band is specifically inhibited with the AMPKα immunizing peptide (amino acids 2-19) in humans.

The 5′-AMP-activated protein kinase (AMPK) is coded by the AMP-activated protein kinase catalytic subunit α-1 gene (PRKAA1). It is located on human chromosome 5p13.1.

This sequence is highly conserved (single amino acid substitution, 2 amino acids deletion) in rat and mouse AMPKα1 and in human, rat and mouse AMPKα2.

synthetic peptide corresponding to amino acids 2-19 located at the N-terminus of human AMPKα1, conjugated to KLH.

Anti-AMPKα antibody is suitable for use in western blot (0.5-1.0μg/mL using whole cell extract of mouse 3T3-L1 adipocytes or human kidney 293 cells).

The 5′-AMP-activated protein kinase (AMPK) participates in the biosynthesis of macromolecules and cellular metabolism. Protein kinase catalytic subunit α-1 gene (PRKAA1), a subunit of the AMPK pathway plays a major role in cellular activity and cancer development. It also participates in cell differentiation, apoptosis, autophagy and in clinical prognosis.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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