| Application | Recommended Dilution |
|---|---|
| FC | 1:50-1:200 |
PRKAR2B encodes the type II-beta regulatory subunit of cAMP-dependent protein kinase (PKA), a central mediator of cellular responses to hormonal and neurotransmitter signals. As a key component of the PKA holoenzyme, PRKAR2B governs the spatial and temporal regulation of kinase activity by sequestering catalytic subunits until cAMP binding triggers their release. This regulatory mechanism places PRKAR2B at the intersection of metabolic control, synaptic plasticity, and endocrine signaling pathways, making it a compelling target for researchers investigating signal transduction networks and their dysregulation in disease states.
This recombinant monoclonal antibody, clone 6D12, offers the reproducibility and molecular definition that demanding experimental workflows require. Developed in rabbit against a synthetic peptide derived from human PRKAR2B, the antibody undergoes affinity chromatography purification to ensure consistent performance across experiments. The recombinant production platform eliminates the lot-to-lot variability inherent to traditional hybridoma-derived antibodies, providing researchers with a sequence-defined reagent they can rely on for longitudinal studies and cross-laboratory comparisons.
Validation for flow cytometry demonstrates clear detection of PRKAR2B in Jurkat cells, a human T lymphocyte line, with recommended working dilutions between 1:50 and 1:200. The intracellular staining protocol employed formaldehyde fixation and Triton X-100 permeabilization, confirming the antibody's suitability for detecting this cytoplasmic target in fixed cell preparations. The antibody is also validated for ELISA applications, offering flexibility for researchers requiring both single-cell and population-level analyses.
This antibody serves investigators exploring PKA signaling dynamics, cAMP-mediated pathways, and the regulatory mechanisms underlying cellular responses to extracellular stimuli.
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