The Recombinant SARS-COV-2 NSP7&NSP8 Protein is a high-quality recombinant protein produced for advanced research applications in molecular biology and biotechnology. This protein serves as a critical reagent in various experimental contexts, including functional studies, binding assays, and therapeutic development programs, providing researchers with a standardized and reliable tool for investigating protein function and interactions.
This product (SKU: RPCB2093) is produced using E. coli and features a C-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 32.8 kDa, achieving ≥ 95 % as determined by Tris-Bis PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant SARS-COV-2 NSP7&NSP8 Protein (RPCB2093), tested reactivity in E. coli and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 1 EU/μg of the protein by LAL method.
Purity:
≥ 95 % as determined by Tris-Bis PAGE.
Reconstitution:
Centrifuge the tube before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
The crystal structure of the metabolite of remdesivir (Monophosphate of GS-441524) and NSP12-NSP8-NSP7 of SARS CoV-2 virus was recently reported. The crystal structures of ADP-Ribose or AMP and NSP3 of SARS CoV-2 virus were also released, recently. The crystal structure of NSP3 of SARS CoV-2 virus as an alternative binding site of AMP or ADP-ribose to treat COVID-19.
Recombinant SARS-COV-2 NSP7&NSP8 Protein was determined by Tris-Bis PAGE under reducing conditions.
