Anti-phospho-AMPK α (pThr¹⁷²) antibody produced in rabbit

AMP-activated protein kinase α (AMPKα) exists in two isoforms α1 and α2. The gene coding for AMPK α1 and AMPKα2 is mapped to human chromosome 5p11-p14 and 1p31 respectively. AMPKα is a 63kDa catalytic subunit of AMPK, involved in regulation of AMP levels. The AMP-activated protein kinase (AMPK) is a ubiquitously expressed cellular energy sensor.

The antiserum was produced against synthesized peptide derived from human AMPK alpha around the phosphorylation site of Thr172.

Immunogen Range: 140-189

Anti-phospho-AMPK α (pThr172) antibody produced in rabbit has been used in western blot analysis.

Anti-phospho-AMPK α (pThr172) antibody produced in rabbit has been used in western blotting.

AMP-activated protein kinase is activated by the increased concentration of adenosine mono phosphate (AMP) during mitochondrial dysfunction. AMPK, or AMPK α1, is a vital constituent of the adaptive response to cardiomyocyte stress that occurs during ischemia. AMPK is involved in regulation of various cellular processes such as mitochondrial biogenesis, autophagy and inflammation, and immune responses. AMPK signaling pathway aids in maintaining energy balance in retinal neurons, therefore, it is considered as a potential therapeutic target to prevent or delay retinal degeneration. AMPK acts as a cellular energy sensor that controls glucose and lipid metabolism in response to change in nutrient and intracellular energy levels. C allele of protein kinase AMP-activated catalytic subunit α 1 (PRKAA1) rs13361707 is associated with susceptibility of gastric cancer (GCa). AMPKα2 plays an essential role in controlling postmortem glycolysis in skeletal muscle.

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Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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