His6-UBE2K, human recombinant

Human UBE2K (HIP-2) is an E2 ubiquitin conjugating enzyme. An E1 activating enzyme is required to attach ubiquitin to UBE2K via an active site cysteine. The mechanism of ubiquitin transfer involves the breaking of a E1-Ub thioester linkage, followed by a reformation of a UBE2K-Ub thioester. UBE2K is capable of synthesizing K-48 linked ubiquitin chains and can do so without an E3 ubiquitin ligating enzyme present. Although an E3 ligase is not required for chain formation, free UBE2K synthesized K48 polyubiquitin chains have been shown to interact with the E3 TRIM6, leading to activation of IKKe kinase activity and subsequent antiviral activity. This recombinant UBE2K is expressed in E.coli with an N-terminal poly-histidine tag. Final purity for this enzyme is > 95% - determined by SDS-PAGE.