PPP2R5E Antibody / PP2A regulatory subunit epsilon, 100 ug

PPP2R5E antibody detects Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform, encoded by the PPP2R5E gene on chromosome 14q23.2. PPP2R5E antibody is used in studies of phosphatase signaling, cell cycle regulation, and cancer. PPP2R5E encodes a regulatory B56 subunit of protein phosphatase 2A (PP2A), a major serine/threonine phosphatase that regulates diverse cellular processes, including signal transduction, apoptosis, and DNA replication. The B56 epsilon subunit directs PP2A holoenzyme localization and substrate specificity.

Structurally, PPP2R5E is a ~55 kDa protein containing HEAT repeat motifs that mediate protein-protein interactions. It associates with the PP2A catalytic C subunit and scaffolding A subunit to form a heterotrimeric holoenzyme. Alternative splicing produces isoforms that regulate localization and target binding. PPP2R5E is primarily nuclear but can localize to the cytoplasm depending on signaling context.

Functionally, PPP2R5E directs PP2A activity toward substrates involved in cell cycle progression, DNA damage response, and Wnt signaling. It has been implicated in regulation of mitotic exit, checkpoint activation, and dephosphorylation of key transcription factors. Researchers use PPP2R5E antibody to study PP2A holoenzyme regulation, signaling networks, and disease mechanisms.

Clinically, alterations in PP2A subunits, including PPP2R5E, have been linked to cancer, where loss of PP2A tumor suppressor activity contributes to abnormal signaling. Dysregulation of PPP2R5E may influence pathways such as Myc stabilization, Akt signaling, and beta-catenin activity. Because PP2A is a critical tumor suppressor, PPP2R5E and other regulatory subunits are being investigated as biomarkers and therapeutic targets. NSJ Bioreagents provides PPP2R5E antibody for research on phosphatase regulation, cell signaling, and cancer biology.

Experimentally, PPP2R5E antibody is applied in western blotting to detect the ~55 kDa protein, in immunohistochemistry to study tissue expression, and in co-immunoprecipitation to identify PP2A holoenzyme partners. It is also used in phosphatase assays to assess regulatory subunit effects on enzymatic activity.