Ubiquitin-conjugating (E2) enzymes are characterized by the presence of a highly conserved ubiquitin-conjugating domain which accommodates ATP-activated ubiquitin (Ub) via a covalently linked thioester onto its active-site residue. E2 enzymes act via selective protein-protein interactions with the ubiquitin-activating E1 enzyme and ubiquitin ligase E3 enzymes and are able to differentiate effects on downstream substrates, either with a single Ub molecule or a Ub chain. While E3s are involved in substrate selection, E2s are the main determinants for selection of the lysine to construct Ub chains, which thereby directly control the cellular fate of the substrate. The UbcH5 family (UbcH5a, UbcH5b and UbcH5c) have been shown to be the most active class of E2 enzymes in cell extracts and are associated with the control of a number of proteins including the transcriptional regulators p53, Ikba and HIF-1A.
Recombinant protein corresponding to full-length active human UbcH5c, fused to 6His-tag at N-terminal HA, expressed in E. coli
Molecular Weight:~19kD
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：10ug
Source Antigen：Recombinant, E. coli
Grade：Highly Purified
Purity：≥99% (SDS-PAGE, Coomassie blue staining)
Form：Supplied as a liquid in 50mM Tris/HCl, pH7.5, 300mM sodium chloride, 0.1mM EGTA, 0.03% Brij-35, 270mM sucrose, 1mM benzamidine, 0.2mM PMSF, 0.1% 2-mercaptoethanol.
