Anti-USP25 Antibody

Raised in rabbit as an unconjugated polyclonal IgG, this primary antibody from Antibodies.com detects Ubiquitin Specific Peptidase 25 (USP25), a deubiquitinating enzyme that cleaves ubiquitin from substrate proteins. The reagent is supplied as a 50 µl liquid aliquot in a single-use vial, validated for western blot (WB), immunohistochemistry (IHC), and immunoprecipitation (IP), and cross-reacts with Human, Mouse, and Rat samples for comparative work in cell lysates and tissue sections.

USP25 has documented roles across several signaling pathways that researchers commonly probe with this reagent. Published studies show that USP25 removes Act1-mediated K63-linked polyubiquitin chains from TRAF5 and TRAF6, restraining IL-17-triggered NF-κB and Jnk activation, and that the enzyme stabilizes tankyrases to sustain Wnt/β-catenin signaling. The enzyme is distributed in the cytoplasm and nucleus, where it influences DNA damage responses and innate antiviral immunity through stabilization of TRAF3 and TRAF6. Two short, ubiquitously expressed isoforms and a longer muscle-specific isoform (USP25m) have been described in the literature.

For best results, aliquot to limit freeze-thaw cycles, store refrigerated, and protect from light. Intended for research use only.