Analytical Data
-
Gene name
UBA52
- Application
-
Alternative Names
CEP52; HUBCEP52; RPL40; 60S Ribosomal Protein L40; Ubiquitin Carboxyl Extension Protein 52
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P62987
-
Expression Region
Met1~Lys128
-
Molecular Weight
18kDa
-
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
UBA52 is a ubiquitin fusion protein that plays a crucial role in the ubiquitin-proteasome system, which is essential for protein degradation and regulation of various cellular processes. UBA52 encodes two functional domains: ubiquitin and ribosomal protein L52, indicating its involvement in both protein modification and ribosome biogenesis. The research on UBA52 has gained attention due to its implications in various biological processes, including cell cycle regulation, stress responses, and apoptosis. Dysregulation of ubiquitin-mediated pathways has been linked to several diseases, including cancer, neurodegenerative disorders, and viral infections. Understanding the function and mechanism of UBA52 can provide insights into its potential roles in these diseases and offer avenues for therapeutic interventions. Recent studies employing advanced techniques such as CRISPR-Cas9 and proteomic analyses are elucidating the interactions and regulatory networks involving UBA52, enhancing our understanding of its biological significance. By investigating the structural and functional properties of UBA52, researchers aim to uncover how this protein modulates cellular functions and contributes to disease pathogenesis, thereby expanding the potential for targeted treatments that harness the ubiquitin-proteasome system.
