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UbcH5c (human), (recombinant) (His-tag)

 
BML-UW9070-0100 100 µg 279.00 USD
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Product Specification

MW:~16kDa
 
Source:Produced in E. coli.
 
UniProt ID:P61077
 
Formulation:Liquid. In TRIS-HCl, pH 7.5, containing 1mM DTT.
 
Purity:≥90% (SDS-PAGE)
 
Biological Activity:The His6-tagged fusion proteins of UbcH5a, UbcH5b and UbcH5c all charge and support ubiquitinylation in vitro. Unlike their GST-tagged counterparts, the His6-tagged UbcH5 family members all appear to form thiol ester conjugates with ubiquitin at a similar rate under similar conditions.
 
Application Notes:Useful for in vitro ubiquitinylation reactions. Typical enzyme concentration to support conjugation in vitro is 100nM to 1μM depending upon conditions. The His-tagged version of this enzyme is not susceptible to self-ubiquitinylation, which can occur with GST-tagged versions.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:A number of E2s in Saccharomyces cerevisiae and their homologues have been identified. One such family of E2s is the UBC4/5, characterised as essential for the degradation of short-lived, regulatory and abnormal proteins. Protein levels of S. cerevisiae UbC4/5 are up-regulated in response to stress, and their loss results in severe effects on cellular functions.

A human gene product that is 79% identical to S. cerevisiae UBC4/5 in amino-acid sequence was identified as UbcH5a. In addition, two other human members of this highly conserved E2 class were also cloned and designated as UbcH5b and UbcH5c, having 88% and 89% identity to UbcH5a, respectively. Members of the UbcH5a/b/c are the most active class of E2s in cell extracts. The importance of this enzyme class is underscored by the critical role of UBC4/5 in S. cerevisiae. UbcH5a stimulates the conjugation of ubiquitin to the tumour-repressor p53 in the presence of E6-AP and E6. Moreover, UbcH5 family is implicated in c-fos recognition, the modulation of which is controlled by the ubiquitin-proteasome pathway. UbcH5b and UbcH5c are associated with the signal-induced conjugation and subsequent degradation of IkBα in the presence of the SCF complexes. UbcH5c also catalyses the ubiquitination leading to the processing of p105 precursor to form p50, a subunit of the heterodimeric transcription factor NF-kB. The range and diversity of substrates and E3s with which this class of E2 enzymes interact, suggest their complex roles in cellular functions require to be studied further.
 
Regulatory Status:RUO - Research Use Only
 

Product Literature References

Biophysical and biological evaluation of optimized stapled peptide inhibitors of the linear ubiquitin chain assembly complex (LUBAC): F. Aguilar-Alonso, et al.; Bioorg. Med. Chem. 26, 1179 (2018), Abstract;
BLM Potentiates c-Jun Degradation and Alters Its Function as an Oncogenic Transcription Factor: R. Priyadarshini, et al.; Cell Rep. 24, 947 (2018), Abstract;
Prp19/Pso4 Is an Autoinhibited Ubiquitin Ligase Activated by Stepwise Assembly of Three Splicing Factors: T.R. de Moura, et al.; Mol. Cell 69, 979 (2018), Abstract;
ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-dependent CRMP2 phosphorylation: S. Wakatsuki, et al.; Nat. Cell Biol. 13, 1415 (2011), Abstract;

General Literature References

Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha: H. Gonen et al.; J. Biol. Chem. 274, 14823 (1999),
Enzymes catalyzing ubiquitination and proteolytic processing of the p105 precursor of nuclear factor kappaB1. : Coux, O. and Goldberg, A.L.; J. Biol. Chem. 273, 8820-8 (1998),
Degradation of the proto-oncogene c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterisation of the conjugating enzymes: I. Stancovski et al.; Mol. Cel. Biol. 15, 7106 (1995),
Identification of a family of closely related human ubiquitin conjugating enzymes: J.P. Jensen et al.; J. Biol. Chem. 270, 30408 (1995),
Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. : Scheffner, M.; Proc. Natl. Acad. Sci. USA 91, 8797-8801 (1994),
The ubiquitin-conjugation system. : Jentsch, S. ; Annu. Rev. Genet. 22, 179-207 (1992),
Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. : Seufert, W. and Jentsch, S.; EMBO J. 9, 543-50 (1990),

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