UbcH5c Protein, active, 10 µg

N-terminal HA, 6His-tagged, recombinant human UbcH5c full length, expressed in E.coli.

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, IκBα and HIF-1α.

Ubiquitination Cascade Comoponent: E2

Purified using immobilized metal affinity chromatography.

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

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