PRKAR2A抗体—艾普蒂

+ +

•  

   

     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-2: HEPG2 cell and Human testis tissue lysates, Primary antibody: P01647(PRKAR2A Antibody) at dilution 1/550, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 30 seconds    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human breast cancer tissue using P01647(PRKAR2A Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human esophagus cancer tissue using P01647(PRKAR2A Antibody) at dilution 1/50. (Original magnification: ×200)    

  
  

The PRKAR2A antibody is a crucial tool for studying the regulatory subunit RIIα of protein kinase A (PKA), a central enzyme in cAMP-mediated signaling pathways. PRKAR2A (cAMP-dependent protein kinase type II-alpha regulatory subunit) plays a key role in anchoring PKA to specific cellular compartments via A-kinase anchoring proteins (AKAPs), ensuring localized phosphorylation events that regulate diverse processes, including metabolism, gene expression, and cell proliferation. This antibody is widely used in Western blotting, immunohistochemistry, and immunofluorescence to detect PRKAR2A expression, which is ubiquitously present in tissues but shows elevated levels in the brain, heart, and skeletal muscle.

Research utilizing PRKAR2A antibodies has elucidated its involvement in diseases such as cardiovascular disorders, endocrine tumors, and Carney complex—a genetic condition linked to PRKAR1A mutations, where PRKAR2A expression may compensate for dysfunctional regulatory subunits. Additionally, PRKAR2A dysregulation has been implicated in cancer progression, with studies highlighting its role in modulating cell cycle checkpoints and apoptosis. Commercially available PRKAR2A antibodies are typically raised in rabbits or mice, targeting specific epitopes within the protein's N-terminal or cAMP-binding domains. Validation includes reactivity checks in knockout models or siRNA-treated cells to ensure specificity. Researchers must optimize protocols for tissue types and fixation methods, as post-translational modifications (e.g., phosphorylation) or isoform cross-reactivity (e.g., PRKAR2B) may affect results. This antibody remains vital for dissecting cAMP-PKA signaling mechanisms in health and disease.