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Catalog Number | orb640158 |
---|---|
Category | Proteins |
Description | The viral nonstructural protein 1 (nsP1) is the only membrane-associated protein that anchors the replication complex to the cellular membranes. NSP1 inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. |
Reactivity | Virus |
Tag | C-10×His |
Form/Appearance | Powder |
Purity | 90% |
Conjugation | Unconjugated |
MW | 21.7 kDa |
Target | NSP1 |
Protein Sequence | YP_009725297.1 |
Source | SARS-CoV-2 NSP1, His Tag (orb640158) is expressed from E. coli cells. It contains AA Met 1 - Gly 180 (Accession # YP_009725297.1). |
Expression System | E. coli |
Expression Region | Met 1 - Gly 180 |
Endotoxins | 1.0 EU per μg |
NCBI | YP_009725297.1 |
Storage | -20℃ |
Buffer/Preservatives | PBS, Arginine, pH7.4 |
Alternative names | NSP1,nsp1,Leader protein,Host translation inhibito Read more... |
Note | For research use only |
Application notes | This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 21.7 kDa. The protein migrates as 22-25 kDa under reducing (R) condition (SDS-PAGE). |
Expiration Date | 6 months from date of receipt. |
ELISA | |
Virus | |
Rabbit | |
Polyclonal | |
Unconjugated |
GSH-Agarose (0.5) | |
Mono-Isotopic Mass: 46, 569.73 daltons Average Mass: 46, 599.47 daltons | |
bacteria |
Amylose Resin (0.6) | |
Mono-Isotopic Mass: 63, 974.47 daltons Average Mass: 64, 014.22 daltons | |
bacteria |
> 85% as determined by SDS-PAGE quantitative densitometry by Coomassie Blue Staining. | |
21.94kDa | |
E. coli |
Greater than 85% as determined by reducing SDS-PAGE. | |
E. coli |
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