Phospho-PKA RIIα (PRKAR2A)-S99 Rabbit mAb for WB and ELISA - P13861

Core Product Specifications and Parameters

Biological Background: PRKAR2A Function and Localization

• PRKAR2A encodes the cAMP-dependent protein kinase type II-alpha regulatory subunit, a key component of the PKA holoenzyme that modulates cellular responses to cAMP.
• As the regulatory subunit of PKA, it binds cAMP, leading to dissociation and activation of the catalytic subunits, which then phosphorylate downstream targets involved in metabolism, gene expression, and cell proliferation.
• Type II regulatory subunits mediate membrane association by binding to A-kinase anchoring proteins (AKAPs), including MAP2 kinase, thereby localizing PKA activity to specific subcellular compartments.
• The human genome contains four regulatory subunit types (I-alpha, I-beta, II-alpha, and II-beta); PRKAR2A belongs to the type II-alpha class, and its expression varies across tissues, being constitutive in some and inducible in others.
• PRKAR2A is predominantly localized in the cytoplasm and can associate with the cell membrane through interactions with anchoring proteins, enabling spatial control of cAMP signaling.
• The protein undergoes post-translational modifications, including phosphorylation at multiple sites (e.g., Ser99) and acetylation, which regulate its activity, stability, or interaction with partners.
• Alternative splicing generates different isoforms, and the protein is classified under keywords such as Phosphoprotein, Acetylation, and cAMP-binding, reflecting its dynamic regulatory roles.

Experimental Guidance and Technical Tips

• The immunogen is a synthetic phosphopeptide around Ser99; consider verifying phospho-specificity by comparing signals between treated and untreated samples or using a non-phosphopeptide blocking control.
• For Western blotting, a band near 46 kDa is expected; optimize blocking and antibody dilution in the relevant sample system, as endogenous expression may vary.
• In ELISA, use the antibody to detect phosphorylated PRKAR2A in cell or tissue lysates; include appropriate positive and negative controls to confirm assay specificity.
• Cross-reactivity is confirmed for human and rat; if using mouse samples, validate cross-reactivity experimentally due to possible sequence differences.
• Due to the critical role of PKA in signaling, phosphorylation at Ser99 may be dynamic; consider stimulating or inhibiting cAMP pathways when designing experiments.

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