A heterodimer composed of the catalytically active ubiquitin-conjugating enzyme UbcH13 and its catalytically inactive paralog hMms2, which lacks an active site cysteine residue.
Product Details
| MW: | ~18.4kDa |
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| Source: | Produced in E. coli. |
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| UniProt ID: | P61088 (UbcH13), Q15819 (Mms2) |
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| Formulation: | Liquid. In 50mM HEPES, pH 8.0, 50mM sodium chloride, 10% glycerol, 1mM DTT. |
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| Purity: | ≥95% (SDS-PAGE) |
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| Application Notes: | Typical enzyme concentration to support conjugation in vitro is 100nM to 1µM depending upon conditions. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Handling: | Avoid freeze/thaw cycles. |
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| Scientific Background: | The UbcH13/Mms2 complex catalyzes synthesis of Lys-linked, ubiquitin chains, which serve as non-proteolytic tags involved in error-free post-replicative DNA repair and NF-κB signal transduction. |
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| Regulatory Status: | RUO - Research Use Only |
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Due to similarities in molecular weight (18.4kDa and 16.4kDa) it is difficult to separate the two components on SDS-PAGE under standard conditions. UW9565 has been characterised in a thiolester assay [in the presence (A) and absence (B) of ATP] using biotinylated ubiquitin (product code UW8705) as shown opposite. Major bands observed are for biotinylated ubiquitin and the biotinyl-ubiquitin thiol ester linked UbcH13 as marked. Please note that, due to the efficiency of ubiquitin transfer under the conditions used, it is not possible to observe the presence of the biotinyl-ubiquitin thiol ester linked E1.
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Product Literature References
BLM Potentiates c-Jun Degradation and Alters Its Function as an Oncogenic Transcription Factor: R. Priyadarshini, et al.; Cell Rep.
24, 947 (2018),
Abstract;
General Literature References
An NMR-based model of the ubiquitinbound human ubiquitin conjugation complex Mms2: S. McKenna et al.; J. Biol. Chem. 278, 13151 (2003),
In vitro assembly and recognition of Lys-63 polyubiquitin chains.: Hofmann, R.M. and Pickart, C.M. ; J. Biol. Chem. 276, 27936-27943 (2001),
Noncanonical MMS2-encoded ubiquitin conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair.: Hofmann, R.M. and Pickart, C.M.; Cell 96, 645-653 (1999),
