Anti-USP25 Antibody

USP25 (ubiquitin specific peptidase 25), also known as USP21, belongs to the peptidase C19 family and is a highly conserved 76-amino acid protein involved in regulation of intracellular protein breakdown, cell cycle regulation, and stress response (1) . It contains one UBA-like domain and two UIM (ubiquitin-interacting motif) repeats. Due to alternative splicing events, USP25 is expressed as two short, ubiquitously expressed isoforms and one long, muscle-specific isoform (2) . The long isoform of USP25 (USP25m) is upregulated in myogenesis and is implicated in regulation of muscular differentiation and function. USP25 is a deubiquitinating enzyme (DUB) that negatively regulates IL-17-triggered signaling (3,4) .

USP25 antibody was raised against a 17 amino acid peptide near the center of human USP25. The immunogen is located within amino acids 470 - 520 of USP25.

Isoform USP25a is found in most adult and fetal tissues; expression is moderately high in testis, pancreas, kidney, skeletal muscle, liver, lung, placenta, brain, heart, but very low in peripheral blood, colon, small intestine, ovary, prostate, thymus and spleen. Isoform USP25b is found in all tissues except heart and skeletal muscle. Isoform USP25m is heart and skeletal muscle specific.

Deubiquitinating enzyme that hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains.