Description

Background
A large family of cysteine proteases known as deubiquitinating enzymes (DUB) is capable of dissociating ubiquitin or ubiquitin-like proteins from proteins that have been conjugated to ubiquitin. Ulp1 peptidase cleaves at the Gly-Gly-↓Ala-Thr-Tyr site downstream of the small ubiquitin-like modifier (SUMO) tag.The optimal temperature for cleavage is 30°C; however, the enzyme is active over wide ranges of temperature (see table on page 3) and pH (pH 7.0–9.0). Following digestion, SUMO Protease is easily removed from the cleavage reaction by affinity chromatography using the polyhistidine tag at the N-terminus of the protease. Ulp1 protease is purified from E. coli by affinity chromatography using the polyhistidine tag.

KUYBIIG-M ULP1 Technical Data Sheet