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UbcH3 (human), (recombinant) (His-tag)

BML-UW8730-0100 100 µg 258.00 USD
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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 (molecular weight 32kDa) involved in the control of cell cycle and DNA replication being homologous to Cdc34 from Saccharomyces cerevisiae. The human CDC34 gene is expressed in multiple cell lines as a unique species and is highly conserved in higher eukaryotes. The gene has been localised to chromosome 19p13.3.  Functional and physical characterisation has been undertaken. It has been demonstrated that the protein itself is a substrate for both ubiquitinylation and phosphorylation. Few in vivo targets of UbcH3 are currently known although investigation continues.

Product Specification

Source:Produced in E. coli.
UniProt ID:P49427
Formulation:Liquid. In HEPES, pH 8.0, containing 50mM NaCl, 1mM DTT, and 10% glycerol.
Purity:≥95% (SDS-PAGE)
Application Notes:Useful for in vitro ubiquitinylation reactions.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Scientific Background: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 vivo11.
Technical Info/Product Notes:GST-SUMO-1 may be used to identify proteins which interact with human SUMO-1 by use of a simple pulldown assay. For example, in the presence of human placental Fraction II, ATP, Mg2+, and DTT, agaroseimmobilised wild type GST-SUMO-1 may be conjugated to placental soluble proteins as well as noncovalently associated SUMO-1-interacting proteins which may subsequently be eluted using thiol reagents. The product is suitable for the discovery of new SUMO-1-protein conjugates and SUMO1-binding proteins including SUMO-1 activating, conjugating and de-conjugating enzymes. GST-SUMO-1[G76A] in which the glycyl residue necessary for conjugation is mutated to an alanyl residue thereby preventing conjugation is supplied as a control reagent.  Typical in vitro concentration for non-rate limiting conjugate formation is 200μM to 1mM depending upon conditions.  Enzyme is stable to multiple freeze/thaw cycles.

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),

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