PPP2R5E Recombinant Monoclonal Antibody

PPP2R5E serves as a critical regulatory subunit of protein phosphatase 2A, one of the most abundant serine/threonine phosphatases in eukaryotic cells. This B56-epsilon subunit directs PP2A holoenzyme substrate specificity and subcellular localization, making it essential for understanding cell cycle regulation, DNA damage responses, and signal transduction pathways. Dysregulation of PP2A regulatory subunits has been implicated in various malignancies, positioning PPP2R5E as a meaningful target for cancer biology and cell signaling research.

This recombinant monoclonal antibody, generated from clone 5B11 in rabbit host, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and production occurs through recombinant expression, researchers can expect reliable performance across experiments and between lots, eliminating the variability often encountered with traditional hybridoma-derived antibodies.

Validation testing demonstrates robust performance across multiple platforms. Western blot analysis successfully detects PPP2R5E in diverse human cell lines including U-251MG, HEK293, COLO-205, HeLa, PC-3, and MCF-7, as well as mouse NIH/3T3 cells, confirming cross-species reactivity with human and mouse samples. The observed band at approximately 50 kDa runs slightly below the predicted 55 kDa molecular weight, a difference commonly attributable to post-translational processing or protein conformation. Immunohistochemistry validation in human lung cancer and testis tissues shows clear staining patterns, while flow cytometry analysis in HeLa cells demonstrates distinct signal separation from isotype controls.

This antibody supports researchers investigating PP2A-mediated signaling, tumor suppressor mechanisms, and phosphatase biology across oncology, cell cycle, and signal transduction applications.