Analytical Data
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Gene name
UBE2W
- Application
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Alternative Names
N-terminus-conjugating E2Ubiquitin carrier protein WUbiquitin-conjugating enzyme 16 ;UBC-16Ubiquitin-protein ligase W
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96B02
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Expression Region
1-151aa
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Molecular Weight
33.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
UBE2W, a member of the ubiquitin-conjugating enzyme family, plays a crucial role in the ubiquitin-proteasome pathway, which is essential for various cellular processes including protein degradation, cell cycle regulation, and DNA repair. Unlike other E2 enzymes, UBE2W is particularly notable for its ability to promote the ubiquitination of substrates in a manner that is essential for the regulation of cellular responses to stress and for maintaining protein homeostasis. Research has indicated that UBE2W’s activity is tightly regulated, and its dysregulation is associated with several diseases, including cancer and neurodegenerative disorders. Understanding the structural and functional aspects of UBE2W can provide insights into its specific mechanisms of action and its interactions with various E3 ligases and substrates. Recent studies have focused on the development and characterization of recombinant UBE2W proteins to further elucidate its role in ubiquitination processes. By utilizing techniques such as X-ray crystallography and mutagenesis, researchers aim to identify critical residues involved in its enzymatic activity and to explore potential therapeutic targets for diseases linked to UBE2W dysfunction. As the field of proteostasis continues to grow, the study of UBE2W presents a promising avenue for discovering novel interventions that could ameliorate the effects of diseases resulting from protein misregulation.
