| Code | CSB-RA805325A172phHU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IF | 1:20-1:200 |
PRKAA2, the catalytic alpha-2 subunit of AMP-activated protein kinase, serves as a critical energy sensor that orchestrates cellular metabolic responses to nutrient availability and stress conditions. Phosphorylation at Thr172 represents the key activating modification that switches on AMPK's kinase activity, making this phospho-specific epitope essential for researchers investigating metabolic regulation, autophagy, and cellular energy homeostasis.
This recombinant monoclonal antibody offers the reproducibility that phospho-protein detection demands. Because recombinant technology produces antibodies from a defined sequence rather than traditional hybridoma methods, you can expect consistent performance across experiments and between lots—particularly valuable when tracking subtle changes in phosphorylation status across treatment conditions or time courses.
Validation studies demonstrate reliable detection in Western blot applications, where the antibody identifies the expected 62 kDa band in 293 whole cell lysates as well as A549 cells treated with Calyculin A or EGF—stimulation conditions that enhance phospho-signal detection. The recommended working dilution range of 1:500 to 1:5000 provides flexibility for optimization across different sample preparations and detection systems. For spatial analysis of AMPK activation, immunofluorescence validation in A549 cells confirms the antibody's utility in fixed cell imaging workflows, with successful staining demonstrated at 1:100 dilution following standard formaldehyde fixation and Triton X-100 permeabilization.
Whether you're mapping metabolic signaling networks, investigating stress response pathways, or characterizing the effects of pharmacological AMPK modulators, this phospho-specific antibody provides a dependable tool for monitoring PRKAA2 activation state in human cell models.
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