PRKAA2 (protein kinase AMP-activated catalytic subunit alpha 2) is a critical component of the AMP-activated protein kinase (AMPK), an energy-sensing enzyme central to maintaining cellular energy homeostasis. AMPK functions as a heterotrimer composed of α (catalytic), β, and γ subunits. The α-subunit exists in two isoforms (α1 and α2), encoded by distinct genes (PRKAA1 and PRKAA2). PRKAA2. located on human chromosome 1p31. encodes the α2 isoform, which exhibits tissue-specific expression, predominating in skeletal muscle, heart, and liver, while PRKAA1 (α1) is ubiquitously expressed.
Antibodies targeting PRKAA2 are essential tools for studying AMPK’s role in metabolic regulation, including glucose uptake, lipid metabolism, and mitochondrial biogenesis. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to detect PRKAA2 expression levels, localization, and activation status (e.g., phosphorylation at Thr172). Researchers employ PRKAA2-specific antibodies to investigate diseases linked to AMPK dysregulation, such as type 2 diabetes, obesity, cardiovascular disorders, and cancer.
Commercial PRKAA2 antibodies are typically raised against epitopes within the N-terminal kinase domain or C-terminal regulatory regions. Validation often includes testing in knockout models or siRNA-mediated knockdown to confirm specificity. Cross-reactivity with PRKAA1 must be ruled out due to structural similarities. Studies using these antibodies have clarified isoform-specific AMPK functions, revealing that PRKAA2 deletion in mice impairs exercise-induced glucose metabolism, highlighting its unique role in energy stress adaptation.