USP2 monoclonal antibody

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. Through the use of a wide range of enzymes that can add or remove Ub, the Ub pathway controls many intracellular processes such as signal transduction, transcriptional activation and cell cycle progression. USP2 (Ub specific peptidase 2), also known as 41 kDa Ub-specific protease, is a 605 amino acid deubiquitinating enzyme that participates in the Ub pathway. Localized to the cytoplasm, USP2 forms a homooligomer and catalyzes the reaction of the Ub C-terminal thioester with water to form Ub and a thiol. USP2 is expressed as two isoforms produced by alternative splicing.

UBP41; Ubiquitin carboxyl-terminal hydrolase 2; 41 kDa ubiquitin-specific protease; Deubiquitinating enzyme 2; Ubiquitin thioesterase 2; Ubiquitin-specific-processing protease 2