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Recombinant Avian infectious bursal disease virus Structural polyprotein, partial

  • 中文名稱:
    Recombinant Avian infectious bursal disease virus Structural polyprotein ,partial
  • 貨號:
    CSB-YP802516AGAO
  • 說明書:
  • 規格:
  • 來源:
    Yeast
  • 其他:
  • 中文名稱:
    Recombinant Avian infectious bursal disease virus Structural polyprotein ,partial
  • 貨號:
    CSB-EP802516AGAO
  • 說明書:
  • 規格:
  • 來源:
    E.coli
  • 其他:
  • 中文名稱:
    Recombinant Avian infectious bursal disease virus Structural polyprotein ,partial
  • 貨號:
    CSB-EP802516AGAO-B
  • 說明書:
  • 規格:
  • 來源:
    E.coli
  • 共軛:
    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.

  • 其他:
  • 中文名稱:
    Recombinant Avian infectious bursal disease virus Structural polyprotein ,partial
  • 貨號:
    CSB-BP802516AGAO
  • 說明書:
  • 規格:
  • 來源:
    Baculovirus
  • 其他:
  • 中文名稱:
    Recombinant Avian infectious bursal disease virus Structural polyprotein ,partial
  • 貨號:
    CSB-MP802516AGAO
  • 說明書:
  • 規格:
  • 來源:
    Mammalian cell
  • 其他:

產品詳情

  • 純度:
    >85% (SDS-PAGE)
  • 基因名:
    N/A
  • Uniprot No.:
  • 別名:
    Structural polyprotein; PP) [Cleaved into: Precursor of VP2; Pre-VP2); Capsid protein VP2; Structural peptide 1; p1; pep46); Structural peptide 2; p2; pep7a); Structural peptide 3; p3; pep7b); Structural peptide 4; p4; pep11); Protease VP4; EC 3.4.21.-; Non-structural protein VP4; NS); Capsid protein VP3]
  • 種屬:
    Avian infectious bursal disease virus (isolate Chicken/UK/UK661/1989) (IBDV) (Gumboro disease virus)
  • 蛋白長度:
    Partial
  • 蛋白標簽:
    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.
  • 產品提供形式:
    Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
    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.
  • 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:
    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.
  • 注意事項:
    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.

產品評價

靶點詳情

  • 功能:
    Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1.; The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures.; Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation.; Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C-terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator.; Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry.; Structural peptide 2 is a small peptide derived from pre-VP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing.; Structural peptide 3 is a small peptide derived from pre-VP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing.
  • 基因功能參考文獻:
    1. Chicken RPL18 in association with VP3 and PKR affect viral replication. PMID: 29273342
    2. A free VP3 C-terminus is essential for the replication of infectious bursal disease virus. PMID: 28189698
    3. Immunoprecipitation experiments demonstrated that protein-protein interactions between chicken VDAC1 and VP3 and between VDAC1 and VP1 play a role in stabilizing the interaction between VP3 and VP1, further promoting infectious bursal disease virus polymerase activity. PMID: 28592532
    4. The interaction of VP3 and RPL4 is involved in regulating the replication of infectious bursal disease virus. PMID: 26415754
    5. Datasuggest positively selected and co-evolving sites in infectious bursal disease virus (Gumboro virus) viral protein 2 (VP2). PMID: 26245145
    6. our findings indicate that the host cell protein CypA interacts with viral VP4 and inhibits the replication of IBDV PMID: 26090438
    7. VP4 Protein is a phosphoprotein and partially contributes to the cleavage of intermediate precursor VP4-VP3 polyprotein. PMID: 26046798
    8. Infectious Bursal Disease Virus VP3 Upregulates VP1-Mediated RNA-Dependent RNA Replication. PMID: 26311889
    9. Taken together, we concluded that CSGalNAcT2, located in the Golgi apparatus, contributed to the replication of IBDV via interaction with VP2. PMID: 25807054
    10. The double mutation D279N/A284T of the VP2 is sufficient to confer cell culture tropism and replication efficiency, but does not necessarily lead to virus attenuation. PMID: 25420540
    11. The birnavirus VP3 protein inhibits antiviral innate immunity via blockage of viral double-stranded RNA binding to the host cytoplasmic RNA detector MDA5. PMID: 25031338
    12. study found a valine (position 321) that modifies the most exposed part of the capsid protein VP2 modified the antigenicity and partially reduced the pathogenicity of isolate 94432; a threonine (position 276) located in the finger domain of VP1 contributed more significantly to attenuation PMID: 23269788
    13. Thus, infectious bursal disease virus VP4-induced suppression of type I interferon is mediated by interaction with GILZ, a protein that appears to inhibit cell responses to viral infection. PMID: 23152515
    14. Characterization the immunogenicity of recombinant VP2 of infectious bursal disease virus containing N-terminal M2e of avian influenza virus. PMID: 22934356
    15. The extent of synonymous codon usage bias in the IBDV-vVP2 gene maybe influence the gene expression level and secondary structure of protein as well as hydrophobicity. PMID: 21216278
    16. Amino acid substitution at position 990 reduced viral replication of the attenuated Gt strain and reduced its efficacy of protection against virulent infectious bursal disease virus Gx challenge in vivo. PMID: 20471998
    17. Results suggest that the basic face of the pVP2 amphipathic alpha-helix interacts with the acidic region of the VP3 C terminus and that this interaction is essential for VP2 acquisition of competent conformations for capsid assembly. PMID: 19933276
    18. Mutations Q253H and A284T of VP2 were mainly responsible for the virulence of infectious bursal disease virus. PMID: 19766142
    19. Suppression of bursal B lymphocyte growth and proliferation. PMID: 15290373
    20. Genetic variant associated with outbreaks of IBD outbreaks despite vaccination in Tunisia. PMID: 15666864
    21. findings show that two peptides, pep11 and pep46, derived from the precursor pVP2 control virus assembly and cell entry PMID: 16160151
    22. molecular and pathogenicity data indicate that a single amino acid mutation from Histidine (H) to Glutamine (Q) or Asparagine (N) at position 253 in VP2 will markedly increase the virulence of an attenuated IBDV PMID: 18502466

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  • 亞細胞定位:
    [Capsid protein VP2]: Virion. Host cytoplasm.; [Capsid protein VP3]: Virion. Host cytoplasm.; [Structural peptide 1]: Virion. Host cytoplasm.; [Structural peptide 2]: Virion. Host cytoplasm.; [Structural peptide 3]: Virion. Host cytoplasm.; [Structural peptide 4]: Virion. Host cytoplasm.
  • 數據庫鏈接:

    KEGG: vg:956509



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