Recombinant Human UbcH5c/UBE2D3 - Ubiquitin Charged Protein

Ubiquitin-conjugating Enzyme H5c (UbcH5c), also known as Ubiquitin­-conjugating Enzyme E2D 3 (UBE2D3), is a member of the yeast Ubc4/5 family of Ubiquitin­conjugating (E2) enzymes. Human UbcH5c/UBE2D3 has a predicted molecular weight of 17 kDa and shares 88% and 89% amino acid sequence identity with the related family members, UbcH5a and UbcH5b, respectively.  In combination with Ubiquitin ligases (E3s) such as CHIP, UbcH5c/UBE2D3 mediates the ubiquitination and subsequent degradation of several regulatory proteins.  For instance, UbcH5c/UBE2D3 is involved in the polyubiquitination and proteasome­mediated degradation of the Nuclear Factor kappaB (NF­ kappa B) inhibitor, I kappa B­ alpha, and is implicated in NF­ kappa B­-dependent inflammation.  UbcH5c/UBE2D3 also mediates the ubiquitination of Histone H2A and PCNA, suggesting that it functions during transcriptional regulation, DNA replication, and DNA damage responses.

This product is an enzymatically generated UbcH5c/UBE2D3-Ubiquitin thioester complex that has been purified to remove E1 Ubiquitin Activating enzyme, uncharged UbcH5c/UBE2D3, free Ubiquitin, and Mg²⁺-ATP.  The product provides a convenient starting material for use in single-turnover "Ubiquitin Discharge Assays," eliminating the need to either inhibit the E1 Ubiquitin Activating enzyme with potentially confounding chemical treatments or remove ATP via enzyme additions.