Product Details
| MW: | ~32kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P49427 |
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| Formulation: | Liquid. In 50 mM HEPES, pH 8.0, containing 50 mM NaCl, 1 mM DTT, and 10% glycerol. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Application Notes: | Useful for in vitro ubiquitinylation reactions. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Scientific Background: | Ubiquitinylation of proteins constitutes an important cellular mechanism for targeting short-lived proteins for degradation by the 26S proteasome. Three classes of enzymes are involved in the conjugation of ubiquitin to proteins. E1, the ubiquitin activating enzyme, activates ubiquitin through the ATP-dependent formation of a high-energy thiol ester bond between the carboxyl terminus of ubiquitin and the active-site cysteine within E1. This E1-activated ubiquitin is transferred to a cysteine residue of an E2, or ubiquitin-conjugating enzyme (UbC). E2 enzymes, either by themselves or in conjunction with E3 enzymes (ubiquitin ligases), then transfer ubiquitin to target proteins forming stable isopeptide bonds resulting in multi-ubiquitin chain formation. It is the diverse combinations of E2-E3 complexes which are thought to define substrate specificity.
UbcH3 is a class II enzyme, homologous to Cdc34 from Saccharomyces cerevisiae, and is important in the control of cell cycle and DNA replication. UbcH3/Cdc34 in association with different E3 complexes, including SCF, has been shown to target many different substrates for ubiquitination and degradation during cell division, signal transduction, and development. UbcH3 substrates that have been characterized include IκB, Wee1, ICERIIγ, p27Xic1. Additionally, substrates such as β-catenin, p21, and is phosphorylated and ubiquitinylated in vivo. |
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| Regulatory Status: | RUO - Research Use Only |
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General Literature References
Human cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis: D. Pati et al.; Mol. Cell Biol. 19, 5001 (1999),
Functional and physical characterisation of the cell cycle ubiquitin-conjugating enzyme CDC34 (UBC3). Identification of a functional determinant within the tail that facilitates CDC34 self-association: C. Ptak et al.; J. Biol. Chem. 269, 26539 (1994),
The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquitinated and phosphorylated in vivo: M.G. Goebl et al.; Mol. Cell Biol. 14, 3022 (1994),
Cloning of the human homolog of the CDC34 cell cycle gene by complementation in yeast: S.E. Plon et. al.; Proc. Natl, Acad. Sci. USA 15, 10484 (1993),
The ubiquitin-conjugation system: S. Jentsch; Annu. Rev. Genet. 26, 179 (1992),
