USP25 Antibody (C-term)

Synthetic Peptide

Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs), 1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.

Polyclonal

29761

Purified Rabbit Polyclonal Antibody (Pab)

The anti-USP25 C-term Pab (Cat. #AP2150b) is used in Western blot to detect USP25 in rat testis tissue lysate (lane 1) and USP25-transfected HeLa cell lysates (lane 2). Transfection data is kindly provided by Dr. B. Pierrat from the Novartis Institute for Biomedical Research (Basel, Switzerland).

1:1000

IHC-P

NP_037528

122218

HUMAN

NP_037528.3