Recombinant Human coronavirus SARS-COV-2 Nsp7 protein is a SARS-CoV-2 Fragment protein, in the 3860 to 3942 aa range, expressed in Escherichia coli, <= 0.1 EU/mg endotoxin level and suitable for SDS-PAGE.
SDS-PAGE
<= 0.1 EU/mg
Escherichia coli
His tag C-Terminus
SDS-PAGE
No
S K M S D V K C T S V V L L S V L Q Q L R V E S S S K L W A Q C V Q L H N D I L L A K D T T E A F E K M V S L L S V L L S M Q G A V D I N K L C E E M L D N R A T L Q
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Replicase polyprotein 1abMultifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.Host translation inhibitor nsp1Inhibits host translation by interacting with binds to the host 40S subunit in ribosomal complexes, including the 43S pre-initiation complex and the non-translating 80S ribosome (PubMed:32680882,PubMed:32908316). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:32680882,PubMed:32908316). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:32680882,PubMed:32979938). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316). By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity).Non-structural protein 2May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.Non-structural protein 3Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Prevents also host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from substrates in vitro (PubMed:32726803). Can play a role in host ADP-ribosylation by binding ADP-ribose (PubMed:32578982).Non-structural protein 4Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.3C-like proteinaseCleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481).Non-structural protein 6Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity). Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938).Non-structural protein 7Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity).Non-structural protein 8Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity).Non-structural protein 9May participate in viral replication by acting as a ssRNA-binding protein.Non-structural protein 10Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.RNA-directed RNA polymeraseResponsible for replication and transcription of the viral RNA genome.HelicaseMulti-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium (By similarity). Binds to host TBK1 and inhibits TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938).Proofreading exoribonucleaseEnzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.Uridylate-specific endoribonucleaseMn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.2'-O-methyltransferaseMethyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.
Replicase polyprotein 1ab, pp1ab, ORF1ab polyprotein, 1a-1b, rep
Recombinant Human coronavirus SARS-COV-2 Nsp7 protein is a SARS-CoV-2 Fragment protein, in the 3860 to 3942 aa range, expressed in Escherichia coli, <= 0.1 EU/mg endotoxin level and suitable for SDS-PAGE.
Replicase polyprotein 1ab, pp1ab, ORF1ab polyprotein, 1a-1b, rep
SDS-PAGE
<= 0.1 EU/mg
Escherichia coli
His tag C-Terminus
SDS-PAGE
No
Yes
Yes
SARS-CoV-2
Reconstitute with phosphate buffered saline.Store lyophilized form at room temperature. Reconstitute, aliquot and store at -80°C for 12 months or +4°C for 1 week.Avoid repeated freeze-thaw. Lyophilized contents may appear as either a translucent film or a white powder. This variance does not affect the quality of the product.
pH: 7.4
Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
S K M S D V K C T S V V L L S V L Q Q L R V E S S S K L W A Q C V Q L H N D I L L A K D T T E A F E K M V S L L S V L L S M Q G A V D I N K L C E E M L D N R A T L Q
Fragment
9.2 kDa
10 kDa
3860 to 3942
Recombinant
His tag C-Terminus
Lyophilized
Equal or greater than 95% by SDS-PAGE.
Replicase polyprotein 1ab
Belongs to the coronaviruses polyprotein 1ab family.
Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed.
Host endosome
Ambient - Can Ship with Ice
Ambient
SARS-CoV-2 nsp7 also known as non-structural protein 7 is an essential component of the coronavirus replication machinery. This protein has a mass of approximately 83 amino acids and is expressed as part of the viral polyprotein after its synthesis in host cells. Nsp7 plays a mechanical role in stabilizing the SARS-CoV-2 replication complex where it acts alongside other non-structural proteins. It is not generated independently but is an integral element within infected host cells facilitating the viral replication process.
The non-structural protein 7 of SARS-CoV-2 participates in forming a protein complex involving nsp8 and nsp12 to enhance viral RNA polymerase activity. This complex contributes to the processivity of the viral polymerase by extending the template RNA facilitating rapid and efficient viral RNA synthesis. Nsp7 through its interactions within this complex ensures the stability and proper functionality of the polymerase during viral replication. Its biological role is therefore indispensable in the production of viral progeny during infection.
The involvement of nsp7 in viral RNA synthesis pathways is significantly linked to the replication and transcription mechanisms of SARS-CoV-2. Nsp7 in tandem with nsp8 modulates the activity of the RNA-dependent RNA polymerase (nsp12) important for the viral life cycle. This pathway directly impacts the replication fidelity and efficiency of SARS-CoV-2 ensuring successful propagation within the host. Through these interactions nsp7 not only stabilizes but also optimizes the function of the replication-transcription complex.
The activity of nsp7 is fundamental in the context of COVID-19 the disease caused by SARS-CoV-2 infection. The protein orchestrates parts of the viral replication process making it an indirect contributor to COVID-19 pathogenesis. Targeting the replication complex formed by nsp7 nsp8 and nsp12 can provide therapeutic strategies to combat COVID-19. The presence of nsp7 within the replication machinery implicates it in disease progression linking it to respiratory syndrome illnesses associated with SARS-CoV-2.
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SDS-PAGE analysis of ab283859 Recombinant Human coronavirus SARS-COV-2 Nsp7. The purity of the protein is ≥95%.
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