| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
Lactate dehydrogenase A (LDHA) serves as a pivotal enzyme in cellular metabolism, catalyzing the interconversion of pyruvate and lactate during anaerobic glycolysis. This metabolic gatekeeper has garnered significant research attention due to its elevated expression in rapidly proliferating cells and its established role in the Warburg effect, making it a compelling target for cancer metabolism studies and therapeutic development.
This recombinant monoclonal antibody against LDHA offers researchers the reproducibility advantages inherent to recombinant technology. Generated from a defined sequence and produced as clone 3E9, it delivers the lot-to-lot consistency essential for longitudinal studies and multi-site collaborations where experimental reproducibility is paramount.
Extensive validation across multiple platforms demonstrates this antibody's versatility in diverse experimental workflows. Western blot analysis confirms robust detection of LDHA at the expected 37 kDa molecular weight across an impressive range of human cell lines, including HepG2, HeLa, Raji, HEK293, A431, and MCF-7, as well as the mouse NIH/3T3 line, confirming the antibody's cross-species reactivity with both human and mouse samples. Immunohistochemistry validation in paraffin-embedded human stomach tissue showcases its utility for examining LDHA expression patterns in archival clinical specimens. Flow cytometry analysis using 786-O renal carcinoma cells further extends its application to single-cell studies, with clear separation from isotype control demonstrating specific intracellular detection.
The unconjugated format and affinity-purified preparation provide flexibility for researchers to pair this antibody with their preferred detection systems. Whether investigating metabolic reprogramming in cancer, exploring glycolytic flux in immune cells, or characterizing LDHA expression in tissue samples, this antibody delivers the specificity and consistency that rigorous research demands.
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