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You are here:Home » Molecular Biology » MB-Peptides » AMP Activated Protein Kinase beta1,2, Human (AMPK- b1,2) Control Peptide

AMP Activated Protein Kinase beta1,2, Human (AMPK- b1,2) Control Peptide


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A 15-aa peptide sequence mapping near the C-terminus of human AMPK-b1/2 (1).
Catalog #A1475-03G
In cells, excess of metabolic fuel is converted into fatty acids in cytosol and oxidized later in mitochondria to generate ATP and acetyl-CoA. In fatty acid synthesis, catalytic formation of malonyl-CoA (precursor for long-chain fatty acyl-CoA, LCFA-CoA) from acetyl-CoA by Acetyl-CoA carboxylase (ACC-1) is the rate limiting step. The translocation of LCFA-CoA from cytosol to mitochondria, catalyzed by two carnitine palmitoyl transferases (CPT-1 & CPT-2) and regulated by ACC-2, is the rate limiting step of mitochondrial fatty acid ?-oxidation. Activities of ACC-1, ACC-2 and other key proteins of carbohydrate and fat metabolism are regulated by their phosphorylation by 5'-AMP-activated protein kinase (AMPK). AMPK switches-off biosynthetic processes when ATP levels are depleted and AMP rises in response to fuel deficiency and treatments like heat shock, ischaemia and exercise. A defect in AMPK switch leads to insulin resistance, dyslipidemia, ketosis resistance and other metabolic derangements in Type 2 diabetes. AMPK also regulates cholesterol biosynthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA resuctase. It also appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathway when ATP levels are depleted and when 5-AMP rises in response to fuel limitation and or hypoxia.
AMPK is a heterotrimer of a catalytic subunit a (~63kD), and two non-catalytic regulatory subunits, b (~40kD) and g (~38kD). These subunits exist in multiple isoforms (a1, a2, b1, b2, g1 and g2). Coexpression of all three subunit is required for kinase activity. AMPK-beta acts as a scaffold vial which trimeric complex of AMPK assembles, with the a-subunit binding to its KIS domain and the g-subunit binding to its KIS domain and the g-subunit binding to its ACS domain. AMPK-beta 1 (mouse/rat/human 270-aa, ~38kD, chromosome 12q24.1) and AMPK Beta-2 (mouse/rat, 271-aa, human 270-aa, ~34kD) share ~70% identity. Both isoform contribute equally to the AMPK activity. AMPK-b1 is highly expressed in liver and brain and low levels in kidney and skeletal muscle. AMPK-b2 is most abundant in skeletal muscle with low levels in kidney, liver, and lung.
SourceHuman synthetic peptide
PurityHighly purified
ConcentrationAs reported
FormSupplied as a liquid in PBS, pH 7.2
Specificity100% conserved in human, mouse and rat AMPK-b1 and AMPK-b2, 93% conserved in drosophila proteins and 100% conserved in C. elegans F55F3.1.p protein (269-aa), Y47D3A.15.p protein (274-aa). Anti-AMPKB11 recognize both b1 and b2 isoform of AMPK. No significant sequence homology seen with AMPK-a or g-isoforms
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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