23-047-M
UbcH7 Protein, active, 10 µg
Active, full length, recombinant human UbcH7. N-terminal HA, 6His-tagged. For use in Enzyme Assays. Functions as an E2 enzyme in ubiquitination assays.
Synonym(s):
Ubiquitin-conjugating enzyme E2 L3, L-UBC, Ubiquitin carrier protein L3, Ubiquitin-conjugating enzyme E2-F1, Ubiquitin-protein ligase L3, UBE2L3, UBCE7
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General description
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 on its active-site residue. E2 enzymes act through 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.
UbcH7 shows broad specificity for HECT-type E3s but does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine. Despite lacking this lysine reactivity, UbcH7 exhibits activity with the RBR family E3 enzymes, such as Parkin and ARIH1.
UbcH7 shows broad specificity for HECT-type E3s but does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine. Despite lacking this lysine reactivity, UbcH7 exhibits activity with the RBR family E3 enzymes, such as Parkin and ARIH1.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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