Recombinant Murine coronavirus Replicase polyprotein 1ab (rep), partial

Code CSB-YP314478MJY
MSDS
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Source Yeast
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Code CSB-EP314478MJY
MSDS
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Source E.coli
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Code CSB-EP314478MJY-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP314478MJY
MSDS
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Source Baculovirus
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Code CSB-MP314478MJY
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
rep
Uniprot No.
Alternative Names
rep; 1a-1b; Replicase polyprotein 1ab; pp1ab; ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1; nsp1; p28); Non-structural protein 2; nsp2; p65); Papain-like proteinase; PL-PRO; EC 3.4.19.12; EC 3.4.22.69; Non-structural protein 3; nsp3; p210); Non-structural protein 4; nsp4; Peptide HD2; p44); 3C-like proteinase; 3CL-PRO; 3CLp; EC 3.4.22.-; M-PRO; nsp5; p27); Non-structural protein 6; nsp6); Non-structural protein 7; nsp7; p10); Non-structural protein 8; nsp8; p22); Non-structural protein 9; nsp9; p12); Non-structural protein 10; nsp10; Growth factor-like peptide; GFL; p15); RNA-directed RNA polymerase; Pol; RdRp; EC 2.7.7.48; nsp12; p100); Helicase; Hel; EC 3.6.4.12; EC 3.6.4.13; nsp13; p67); Guanine-N7 methyltransferase; ExoN; EC 2.1.1.-; EC 3.1.13.-; nsp14); Uridylate-specific endoribonuclease; EC 3.1.-.-; NendoU; nsp15; p35); 2'-O-methyltransferase; EC 2.1.1.-; nsp16)]
Species
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; 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.; May 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.; Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.; Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.; Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.; 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.; 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.; May participate in viral replication by acting as a ssRNA-binding protein.; Plays 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.; Responsible for replication and transcription of the viral RNA genome.; Multi-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.; Enzyme 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.; Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR. Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors.; Methyltransferase 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.
Gene References into Functions
  1. These data show that neither the PLP1 nor the ADRP domain of nsp3 plays an essential role in coronavirus RNA synthesis PMID: 25810552
  2. Authors purified wild-type and ubiquitin-like domain mutant PLP2 and found that the proteases exhibit similar specific activities at 25 degrees C, however, the thermal stability of the Ubl mutant PLP2 was significantly reduced at 30 degrees C. PMID: 25694594
  3. The results also suggest that nsp4 glycosylation serves roles in replication in addition to the organization and stability of murine hepatitis virus-induced double-membrane vesicles. PMID: 25473044
  4. Infection of mice with the macrodomain catalytic point mutant virus (N1347A) resulted in reductions in lethality, weight loss, viral titers, proinflammatory cytokine and chemokine expression, and immune cell infiltration in the brain. PMID: 25428866
  5. The findings demonstrate that long-distance communication pathways between multiple residues and domains of nsp5 play a significant role in nsp5 activity and viral replication. PMID: 22345451
  6. PLP2(papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59) may also target TANK-binding kinase-1 (TBK1), the upstream kinase of IRF3 in the IFN signaling pathway. PMID: 21364999
  7. The experiments have defined residues in ORF 1b and ORF 2a that attenuate virus replication and virulence in mice but do not affect in vitro replication. PMID: 15731233
  8. murine hepatitis virus nsp1 and nsp14 have roles in virus replication PMID: 17037504
  9. analysis of MHV-A59 replicase protein-nsp10 PMID: 17037505
  10. ORF1a replicase protein nsp7-nsp10 processing has roles in virus replication PMID: 17037513
  11. nsp10 is a critical regulator of coronavirus RNA synthesis and may play an important role in polyprotein processing PMID: 17392363
  12. The requirement for the nsp7 to nsp10 proteins and their processing during murine hepatitis virus (MHV) replication was determined. PMID: 17634238
  13. nsp14 ExoN plays a critical role in prevention or repair of nucleotide incorporation errors during genome replication. PMID: 17804504
  14. The experiments identify important residues and regions for studies of nsp4 topology, function, and interactions. PMID: 17855548
  15. These results demonstrate that mNsp15 endoribonuclease is required for optimal infection by MHV. PMID: 17898055
  16. These results reveal a critical role of nsp4 in directing coronavirus double membrane vesicles assembly. PMID: 18295294
  17. Study provides evidence that Papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, can bind to IRF3, cause its deubiquitination and prevent its nuclear translocation. PMID: 18957937
  18. Analysis of nsp6 transmembrane topology revealed six membrane-spanning segments and a conserved hydrophobic domain in the C-terminal cytosolic tail. PMID: 19386712

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Subcellular Location
[Papain-like proteinase]: Host membrane; Multi-pass membrane protein.; [Non-structural protein 4]: Host membrane; Multi-pass membrane protein.; [Non-structural protein 6]: Host membrane; Multi-pass membrane protein.; [Non-structural protein 7]: Host cytoplasm, host perinuclear region.; [Uridylate-specific endoribonuclease nsp15]: Host cytoplasm, host perinuclear region.
Protein Families
Coronaviruses polyprotein 1ab family
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