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UbcH5b (human), (recombinant) (His-tag)

BML-UW9060-0100 100 µg 339.00 USD
BML-UW9060-1000 1 mg 2,886.00 USD
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Product Details

Source:Produced in E. coli.
UniProt ID:P62837
Formulation:Liquid. In 25mM TRIS-HCl, pH 7.5, containing 150mM NaCl and 0.5mM 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. The [C85A] mutation (Prod. No. BML-UW9065) completely abolishes the ability of the enzyme to form a thiol ester and thereby acts as an excellent negative control.
Application Notes:Useful for in vitro ubiquitinylation reactions. The His-tagged version of this enzyme is not susceptible to self-ubiquitinylation, which can occur with GST-tagged versions.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:Enzyme is stable to multiple freeze/thaw cycles.
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
UbcH5b (human), (recombinant) (His-tag) SDS-PAGE
SDS-PAGE analysis: Lane 1: MW Marker, Lane 2: 1 µg UbcH5b (human), (recombinant) (His-tag).
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UbcH5b (human), (recombinant) (His-tag) SDS-PAGE

Product Literature References

Pepper E3 ligase CaAIRE1 promotes ABA sensitivity and drought tolerance by degradation of protein phosphatase CaAITP1: W. Baek, et al.; J. Exp. Bot. 138, 1093 (2021), Abstract;
UBXN2A enhances CHIP-mediated proteasomal degradation of oncoprotein mortalin-2 in cancer cells: S. Sane, et al.; Mol. Oncol. 12, 1753 (2018), Abstract; Full Text
Modulating cellular balance of Rps3 mono-ubiquitination by both Hel2 E3 ligase and Ubp3 deubiquitinase regulates protein quality control: Y. Jung, et al.; Exp. Mol. Med. 49, e390 (2017), Abstract; Full Text
The Pepper RING-Type E3 Ligase CaAIRF1 Regulates ABA and Drought Signaling via CaADIP1 Protein Phosphatase Degradation: C.W. Lim, et al.; Plant Physiol. 173, 2323 (2017), Abstract; Full Text
Identification and functional expression of the pepper RING type E3 ligase, CaDTR1, involved in drought stress tolerance via ABA-mediated signalling: H. Joo, et al.; Sci. Rep. 6, 30097 (2016), Application(s): In vitro ubiquitination, Abstract; Full Text
Loss of NEDD4 contributes to RTP801 elevation and neuron toxicity: implications for Parkinson's disease: M. Canal, et al.; Oncotarget 7, 58813 (2016), Abstract; Full Text
Regulation of the Abundance of Kaposi's Sarcoma-Associated Herpesvirus ORF50 Protein by Oncoprotein MDM2: T.H. Chang, et al.; PLoS Pathog. 12, e1005918 (2016), Abstract; Full Text
Comprehensive functional characterization of cancer-testis antigens defines obligate participation in multiple hallmarks of cancer: K.E. Maxfield, et al.; Nat. Commun. 6, 8840 (2015), Application(s): In vitro autoubiquitination assays, Abstract;
UBXN2A regulates nicotinic receptor degradation by modulating the E3 ligase activity of CHIP: Y. Teng, et al.; Biochem. Pharmacol. 97, 518 (2015), Application(s): Ubiquitinylation, 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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