UbcH3 Protein, active, 10 µg

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 an 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.
UbcH3 has been shown to interact with a number of different E3 ligases, including SCF^Skp2/Cks1, promoting the ubiquitination of p27 and SCF^βTrCP1, promoting the ubiquitination of β-catenin and IκBα.

Active, full length, recombinant human UbcH3. N-terminal HA, 6His-tagged. For use in Enzyme Assays. Functions as an E2 enzyme in ubiquitination assays.

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

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