Analytical Data
-
Gene name
BRCC2
- Application
-
Alternative Names
BH3-like motif containing; cell death inducer; BH3-like motif-containing cell death inducer
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8IZY5
-
Expression Region
1-108aa
-
AA Sequence
MVTLLPIEGQEIHFFEILESECVLYTGWIERASGSSIYPEAKARLPLEALLGSNKEPMLPKETVLSLKRYNLGSSAMKRNVPGHVLQRPSYLTRIQVTLLCNSSAEAL
-
Molecular Weight
39 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
BRCC2 is a critical protein implicated in the DNA damage response, specifically in the regulation of homologous recombination repair pathways. Recent studies have highlighted its role in maintaining genomic stability, particularly in cells subjected to oxidative stress and various DNA-damaging agents. Due to its involvement in cancer progression, BRCC2 has garnered attention as a potential biomarker and therapeutic target, especially in malignancies associated with BRCA mutations. The elucidation of BRCC2's structure, function, and interaction with other proteins is paramount for understanding its mechanism in cellular repair processes. To facilitate this research, the expression and purification of recombinant BRCC2 protein have become essential, enabling detailed biochemical and biophysical characterization. This advances our comprehension of how BRCC2 contributes to DNA repair mechanisms and its potential exploitation in targeted cancer therapies, offering new avenues for intervention in treatment-resistant tumors. Furthermore, structural studies of BRCC2 could reveal novel insights into its regulation and interactions, paving the way for the development of small-molecule inhibitors that specifically modulate its activity in cancer cells. Overall, the recombinant BRCC2 protein research not only enhances our understanding of DNA repair but also holds promise for innovative cancer treatment strategies.
