Analytical Data
-
Gene name
UBE2Q2
- Application
-
Alternative Names
Ubiquitin carrier protein Q2Ubiquitin-protein ligase Q2
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WVN8
-
Expression Region
1-375aa
-
Molecular Weight
58.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
UBE2Q2, a member of the Ubiquitin-conjugating enzyme (E2) family, plays a critical role in the ubiquitin-proteasome system, which is essential for protein degradation and regulation of various cellular processes. Research has shown that UBE2Q2 is involved in the ubiquitination of substrates linked to cell cycle regulation, DNA damage response, and apoptosis. Dysregulation of this enzyme has been implicated in various diseases, including cancer and neurodegenerative disorders. Given its pivotal role, studying UBE2Q2 at the molecular level can provide insights into its function and regulation, and potentially unveil new therapeutic targets. The development and characterization of recombinant UBE2Q2 proteins have facilitated exploration of its biochemical properties, substrate specificity, and interaction with E3 ligases. Furthermore, understanding the structural features of UBE2Q2 can shed light on its mechanism of action and involvement in pathogenic processes. Overall, this research is crucial for elucidating the role of UBE2Q2 in health and disease, potentially leading to novel strategies for intervention in related disorders.
