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Catalog number: SBB-DE0129, 50 μg
The human SARS-CoV-2 coronavirus harbors two proteases Papain Like Protease PLpro and 3CLpro (Chymotrypsin like Protease) or Mpro (Main-Protease) which is a C30-type cysteine protease. The viral genome encodes more than 20 proteins, with 3CLpro located within the non-structural protein 5 (nsp5) section of the viral polypeptide that cleaves together with PLpro polyproteins (PP1A and PP1AB) into individual functional components. 3CLpro recognizes the peptide sequence LQ[S/A/G] where it cleaves c-terminal to the amino acid glutamine (use product SBB-PS0130, KTSAVLQ-Rh110-Glu as universal substrate). The protease 3CLpro is a potential drug target for coronavirus infections due to its essential role in processing the polyproteins that are translated from the viral RNA. The X-ray structures of the unliganded SARS-CoV-2 protease 3CLpro and its complex with an α-ketoamide inhibitor provides a basis for design of α-ketoamide inhibitors. This SARS Coronavirus recombinant 3CLpro is N-terminally His10-tagged and expressed in E.coli.
$189.00
Catalog number: SBB-DE0129, 50 μg
The human SARS-CoV-2 coronavirus harbors two proteases Papain Like Protease PLpro and 3CLpro (Chymotrypsin like Protease) or Mpro (Main-Protease) which is a C30-type cysteine protease. The viral genome encodes more than 20 proteins, with 3CLpro located within the non-structural protein 5 (nsp5) section of the viral polypeptide that cleaves together with PLpro polyproteins (PP1A and PP1AB) into individual functional components.
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$189.00
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| Quantity: | 50 µg |
|---|---|
| Molecular Weight: | 35.6 kDa |
| Purity: | >98% by SDS-PAGE |
| Storage Buffer: | 50 mM HEPES pH 7.5, 100 mM NaCl, 1 mM TCEP |
| Storage | Store at −80°C after product arrival. Avoid multiple freeze/thaws. |
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Open Certificate in New TabCitations and References
1) Fran Robson et al. “Coronavirus RNA Proofreading: Molecular Basis and Therapeutic Targeting”. Molecular Cell, VOLUME 79, ISSUE 5, P710-727, SEPTEMBER 03, 2020, https://doi.org/10.1016/j.molcel.2020.07.027 2) Linlin Zhang et al. “Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors”. SCIENCE • 20 Mar 2020 • Vol 368, Issue 6489 • pp. 409-412 • DOI: 10.1126/science. abb3405 3) Kiemer, L., Lund, O., Brunak, S. et al. Coronavirus 3CLproproteinase cleavage sites: Possible relevance to SARS virus pathology. BMC Bioinformatics 5, 72 (2004). https://doi.org/10.1186/1471-2105-5-72 4) Chen YW, Yiu CPB and Wong KY. Prediction of the SARS-CoV-2 (2019-nCoV) 3C-like protease (3CLpro) structure: virtual screening reveals velpatasvir, ledipasvir, and other drug repurposing candidates [version 2; peer review: 3 approved]. F1000Research 2020, 9:129 (https:// doi.org/10.12688/f1000research.22457.2) 5) Ocain TD et al. “alpha-Keto amide inhibitors of aminopeptidases”. Journal of Medicinal Chemistry. (February 1992). 35 (3): 451–6. doi:10.1021/jm00081a005.
