SARS-COV-2 NSP7&NSP8 Protein 4364

$345.00 – $1,150.00

Summary

Expression: E.coli
Pure: Yes (SDS-PAGE)
Amino Acid Range: Ser1-Gln83(NSP7) & Ala1-Gln198(NSP8)

SKU: 4364parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	YP_009725303(NSP7)&YP_009725304(NSP8)
express system	E.coli
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE
background	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.
molecular weight	The protein has a predicted MW of 32.8 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

SARS-COV-2 NSP7&NSP8 Protein 4364

protein
https://www.uniprot.org/uniprotkb/P0DTC1/
Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
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.
Protein names Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like protease nsp3 (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-stru
Protein family Coronaviruses polyprotein 1ab family
Mass 489989Da
Catalytic activity CATALYTIC ACTIVITY: [Papain-like protease nsp3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269\|PubMed:32726803}; CATALYTIC ACTIVITY: [3C-like proteinase nsp5]: Reaction=TSAVLQ-\|-SGFRK-NH2 and SGVTFQ-\|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000269\|PubMed:32198291, ECO:0000269\|PubMed:32272481, ECO:0000269\|PubMed:32321856}; CATALYTIC ACTIVITY: [RNA-capping enzyme subunit nsp9]: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000269\|PubMed:35944563}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014; Evidence={ECO:0000269\|PubMed:35944563};
Structure SUBUNIT: [Non-structural protein 2]: Interacts with host PHB and PHB2. {ECO:0000250\|UniProtKB:P0C6X7}.; SUBUNIT: [Papain-like protease nsp3]: May form homohexamers (PubMed:32763915). Interacts with N protein (PubMed:35044811). {ECO:0000269\|PubMed:32763915, ECO:0000269\|PubMed:35044811}.; SUBUNIT: [3C-like proteinase nsp5]: 3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity. {ECO:0000269\|PubMed:32198291}.; SUBUNIT: [Non-structural protein 4]: Interacts with PL-PRO and nsp6. {ECO:0000250\|UniProtKB:P0C6X7}.; SUBUNIT: [Non-structural protein 6]: Forms homodimers (PubMed:35551511). Interacts with host ZFYVE1 (DFCP1) (PubMed:35551511), which leads to ER and DMVs binding to lipid droplets. Interacts with host TBK1; this interaction decreases IRF3 phosphorylation by 57%, which leads to reduced IFN-beta production. {ECO:0000269\|PubMed:32979938, ECO:0000269\|PubMed:35551511}.; SUBUNIT: [Non-structural protein 7]: Interacts with nsp8 and nsp12 to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity). {ECO:0000250\|UniProtKB:P0C6X7, ECO:0000269\|PubMed:32277040, ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32438371, ECO:0000269\|PubMed:32526208, ECO:0000305\|PubMed:34562452}.; SUBUNIT: [Non-structural protein 8]: Interacts with nsp7, nsp13 and nsp12 (PubMed:33232691) to form the replication-transcription complex (RTC): nsp12, nsp7, two subunits of nsp8, and up to two subunits of nsp13 (PubMed:32277040, PubMed:32358203, PubMed:32438371, PubMed:32526208, PubMed:34562452). Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (By similarity). {ECO:0000250\|UniProtKB:P0C6X7, ECO:0000269\|PubMed:32277040, ECO:0000269\|PubMed:32358203, ECO:0000269\|PubMed:32438371, ECO:0000269\|PubMed:32526208, ECO:0000269\|PubMed:33232691, ECO:0000305\|PubMed:34562452}.; SUBUNIT: [RNA-capping enzyme subunit nsp9]: Is a dimer (By similarity). Interacts with NSP12 (PubMed:35944563). {ECO:0000250\|UniProtKB:P0C6X7, ECO:0000269\|PubMed:35944563}.; SUBUNIT: [Non-structural protein 10]: Forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. {ECO:0000250\|UniProtKB:P0C6X7}.
Post-translational modification PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed. {ECO:0000250\|UniProtKB:P0C6X7}.
Target Relevance information above includes information from UniProt accession: P0DTC1
The UniProt Consortium

Data

SDS-PAGE gel of SARS-COV-2 NSP7&NSP8 Protein

SARS-COV-2 NSP7&NSP8 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.