Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi ania complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes Lys-11-linked polyubiquitination. Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2. Source: Recombinant protein corresponding to aa1-151 from human UBE2W, fused to His-SUMO-Tag at N-terminal, expressed in E. coli. Molecular Weight: ~33.3kD Amino Acid Sequence: MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC Storage and Stability: Lyophilized and reconstituted products are stable for 6 months after receipt at -20C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Supplied as a lyophilized powder from 20mM Tris-HCl, 0.5M sodium chloride, pH 8.0, 6% trehalose. Reconstitute with sterile ddH2O to a concentration of 0.1-1mg/ml.
* Mehrwertsteuer und Versandkosten nicht enthalten. Irrtümer und Preisänderungen vorbehalten
