UBE2W Protein, Human (His)

UBE2W protein is a multifunctional ubiquitin-conjugating enzyme that accepts ubiquitin in the E1 complex and catalyzes its covalent attachment to different substrates. Notably, UBE2W uniquely monoubiquitylates the N-terminus, including ATXN3, MAPT/TAU, POLR2H/RPB8, and STUB1/CHIP, showing specificity for disordered N-termini. UBE2W Protein, Human (His) is the recombinant human-derived UBE2W protein, expressed by E. coli , with N-His labeled tag.

UBE2W, a versatile ubiquitin-conjugating enzyme, fulfills a crucial role in cellular processes by accepting ubiquitin from the E1 complex and catalyzing its covalent attachment to diverse substrates (PubMed:20061386, PubMed:21229326). Notably, UBE2W exhibits a unique ability to monoubiquitinate the N-terminus of various substrates, including ATXN3, MAPT/TAU, POLR2H/RPB8, and STUB1/CHIP, showcasing its specificity for disordered N-termini (PubMed:23560854, PubMed:23696636, PubMed:25436519). This monoubiquitination process plays a critical role in the degradation of misfolded chaperone substrates, as UBE2W mediates the monoubiquitination of STUB1/CHIP, leading to the recruitment of ATXN3 and restriction of the ubiquitin chain length attached to STUB1/CHIP substrates (PubMed:23696636, PubMed:25436519). Moreover, UBE2W, particularly activated by UV irradiation, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex, collaborating with E3 ubiquitin-protein ligase FANCL to catalyze monoubiquitination of FANCD2, a crucial step in the DNA damage response pathway (PubMed:19111657, PubMed:21229326). In addition to its versatile monoubiquitination capabilities, UBE2W can catalyze 'Lys-11'-linked polyubiquitination in vitro, demonstrating its flexibility in ubiquitin chain formation (PubMed:25436519).

Under ATP and E1 conditions, UBE2W binds with ubiquitin molecules to form thioester complexes UBE2W-Ub.

Human

E. coli

N-His

Q96B02-1 (M1-C151)

55284  [NCBI]

Full Length of Isoform-1

MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC

Approximately 18 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

1.Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.