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Recombinant Sindbis virus Non-structural polyprotein, partial

In Stock
  • 貨號:
    CSB-EP361019SHZ
  • 規格:
    ¥3324
  • 圖片:
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他:

產品詳情

  • 純度:
    Greater than 85% as determined by SDS-PAGE.
  • 基因名:
    N/A
  • Uniprot No.:
  • 種屬:
    Sindbis virus (SINV)
  • 蛋白長度:
    Partial
  • 來源:
    E.coli
  • 分子量:
    60.4 kDa
  • 表達區域:
    1348-1896aa
  • 氨基酸序列
    APSYRTKRENIADCQEEAVVNAANPLGRPGEGVCRAIYKRWPTSFTDSATETGTARMTVCLGKKVIHAVGPDFRKHPEAEALKLLQNAYHAVADLVNEHNIKSVAIPLLSTGIYAAGKDRLEVSLNCLTTALDRTDADVTIYCLDKKWKERIDAALQLKESVTELKDEDMEIDDELVWIHPDSCLKGRKGFSTTKGKLYSYFEGTKFHQAAKDMAEIKVLFPNDQESNEQLCAYILGETMEAIREKCPVDHNPSSSPPKTLPCLCMYAMTPERVHRLRSNNVKEVTVCSSTPLPKHKIKNVQKVQCTKVVLFNPHTPAFVPARKYIEVPEQPTAPPAQAEEAPEVVATPSPSTADNTSLDVTDISLDMDDSSEGSLFSSFSGSDNSITSMDSWSSGPSSLEIVDRRQVVVADVHAVQEPAPIPPPRLKKMARLAAARKEPTPPASNSSESLHLSFGGVSMSLGSIFDGETARQAAVQPLATGPTDVPMSFGSFSDGEIDELSRRVTESEPVLFGSFEPGEVNSIISSRSAVSFPLRKQRRRRRSRRTEY
    Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
    If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
  • 蛋白標簽:
    Tag-Free
  • 產品提供形式:
    Liquid or 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.
  • 緩沖液:
    If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
  • 復溶:
    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.
  • 儲存條件:
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質期:
    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.
  • 貨期:
    3-7 business days
  • 注意事項:
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA:
    Please contact us to get it.

產品評價

靶點詳情

  • 功能:
    Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.; The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. Polyprotein P123 is a short-lived polyprotein that accumulates during early stage of infection. As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins.; The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).; Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase. mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (Probable). NsP1 is needed for the initiation of the minus-strand RNAs synthesis. Probably serves as a membrane anchor for the replication complex composed of nsP1-nsP4. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell.; Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities. NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates. The C-terminus harbors a protease that specifically cleaves the polyproteins and releases the mature proteins. Required for the shutoff of minus-strand RNAs synthesis. Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1. Also inhibits host transcription by inducing rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).; Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis. Displays mono-ADP-ribosylhydrolase activity. ADP-ribosylation is a post-translantional modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication. Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs. The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA.; Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (Probable). Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA.; RNA dependent RNA polymerase. Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs. The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs. The core catalytic domain of nsP4 also possesses terminal adenylyltransferase (TATase) activity that is probably involved in maintenance and repair of the poly(A) tail, an element required for replication of the viral genome.
  • 基因功能參考文獻:
    1. plays an important role in regulating Sindbis virus-induced type I interferon responses PMID: 20097400
    2. These results implicate nsP2 in regulation of minus-strand synthesis and suggest that different regions of the nsP2 MTase-like domain differentially modulate host defense mechanisms, independent of its role as the viral protease. PMID: 18495773
    3. The nsP2-726 Pro residue regulates virus-host cell interactions directly and is also important in viral pathogenesis. PMID: 19428754
    4. These results show that nsP2 (and possibly nsP3) possesses functions other than those needed solely for replication-transcription complex (RTC) activity and that it may also act to regulate minus-strand synthesis and the stability of the RTC. PMID: 19515769
    5. PARP-1 interacts with the C-terminal domain of nsP3 during virus amplification. PMID: 19515826
    6. results revealed new information about the structure of SINV nsP2 and interaction of its domains PMID: 19570872

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  • 亞細胞定位:
    [Polyprotein P1234]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [Polyprotein P123']: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [Polyprotein P123]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [mRNA-capping enzyme nsP1]: Host cytoplasmic vesicle membrane; Lipid-anchor. Host cell membrane; Lipid-anchor; Cytoplasmic side. Host cell projection, host filopodium.; [Protease nsP2]: Host cytoplasmic vesicle membrane; Peripheral membrane protein. Host nucleus. Host cytoplasm.; [Non-structural protein 3]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [Non-structural protein 3']: Host cytoplasmic vesicle membrane; Peripheral membrane protein.; [RNA-directed RNA polymerase nsP4]: Host cytoplasmic vesicle membrane; Peripheral membrane protein.
  • 數據庫鏈接:

    KEGG: vg:1502154



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