UbcH5c, Active, Recombinant, Human, 6-His-Tag (Ubiquitin-conjugating Enzyme E2 D3, Ubiquitin Carrier Protein D3, Ubiquitin-conjugating Enzyme E2(17)KB 3, Ubiquitin-conjugating Enzyme E2-17kD 3, Ubiquitin-protein Ligase D3, UBE2D3, UBC5C)

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, Ikba and HIF-1A.\n\nSource:\nRecombinant corresponding to full-length human UbcH5c, active, fused to 6His-tag at N-terminal HA, expressed in E.coli.\n\nMolecular Weight: \n~19kD\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

029633

Size

10ug

Reactivities

Hum

Form

Supplied as a liquid in 50mM Tris/HCl pH7.5, 300mM sodium chloride, 0.1mM EGTA, 0.03% Brij-35, 270mM sucrose, 1mM benzamidine, 0.2mM PMSF, 0.1% 2-mercaptoethanol.

Purity

~99% (SDS-PAGE, Coomassie blue staining)

References

1. Sadowski M. and Sarcevic B. Mechanisms of Mono- and Poly-Ubiquitination: ubiquitination specificity depends on compatibility between the E2 catalytic core and amino acid residues proximal to the lysine. Cell Division, 5: 19, 2010. 2. Wenzel D.M. et al. E2s: Structurally Economical and Functionally Replete. Biochem. J., 443: 31-42, 2011 van Wijk S. J. L and Timmers H. T. M. The Family of Ubiquitin-Conjugating Enzymes (E2s):deciding between life and death of proteins. The FASEB Journal, 24: 981-993, 2010. 3. Saville M.K. et al., Regulation of p53 by the Ubiquitin-Conjugating Enzymes UbcH5B/C in vivo. J Biol Chem, 279: 42169-42181, 2004. 4. Gonen H. et al., Identification of the Ubiquitin Carrier Proteins, E2s, Involved in Signal-Induced Conjugation and Subsequent Degradation of IkappaBalpha. J Biol Chem. 274: 14823-14830, 1999.