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  4. Recombinant Vesicular stomatitis Indiana virus Glycoprotein G (G), partial

Recombinant Vesicular stomatitis Indiana virus Glycoprotein G (G), partial

  • 中文名稱：
    Recombinant Vesicular stomatitis Indiana virus Glycoprotein G(G) ,partial
  • 貨號(hào)：
    CSB-YP356071VBJ1
  • 規(guī)格：
  • 來源：
    Yeast
  • 其他：
  • 中文名稱：
    Recombinant Vesicular stomatitis Indiana virus Glycoprotein G(G) ,partial
  • 貨號(hào)：
    CSB-EP356071VBJ1
  • 規(guī)格：
  • 來源：
    E.coli
  • 其他：
  • 中文名稱：
    Recombinant Vesicular stomatitis Indiana virus Glycoprotein G(G) ,partial
  • 貨號(hào)：
    CSB-EP356071VBJ1-B
  • 規(guī)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 Vesicular stomatitis Indiana virus Glycoprotein G(G) ,partial
  • 貨號(hào)：
    CSB-BP356071VBJ1
  • 規(guī)格：
  • 來源：
    Baculovirus
  • 其他：
  • 中文名稱：
    Recombinant Vesicular stomatitis Indiana virus Glycoprotein G(G) ,partial
  • 貨號(hào)：
    CSB-MP356071VBJ1
  • 規(guī)格：
  • 來源：
    Mammalian cell
  • 其他：

產(chǎn)品詳情

  • 純度：
    >85% (SDS-PAGE)
  • 基因名：
    G
  • Uniprot No.：
  • 別名：
    G; Glycoprotein
  • 種屬：
    Vesicular stomatitis Indiana virus (strain San Juan) (VSIV)
  • 蛋白長度：
    Partial
  • 蛋白標(biāo)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(chǎn)品提供形式：
    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.
  • 復(fù)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(chǔ)存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)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(xiàng)：
    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(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

  • 功能：
    Attaches the virus to host LDL receptors, inducing clathrin-dependent endocytosis of the virion.; In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane.
  • 基因功能參考文獻(xiàn)：
    1. Vesicular stomatitis virus G protein complex with two distinct cysteine-rich domains (CR2 and CR3) of LDL-R. PMID: 29531262
    2. This work reveals the range of glycoprotein G structural changes and suggests that G monomers can re-associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process. PMID: 28188244
    3. NSF deficiency in HeLa cells barely affected cell viability, anterograde trafficking of vesicular stomatitis virus glycoprotein G and transferrin endocytosis. PMID: 27995606
    4. MARCH8 is highly expressed in terminally differentiated myeloid cells, and that it is a potent antiviral protein that targets viral envelope glycoproteins and reduces their incorporation into virions. PMID: 26523972
    5. Pepscan mapping of autophagy-inducing linear determinants of glycoproteins viral hemorrhagic septicemia virus and glycoproteins vesicular stomatitis virus showed that peptides located in their fusion domains induce autophagy PMID: 25046110
    6. Overall, these results showed that the HIV Env membrane-proximal external region could functionally substitute for the vesicular stomatitis virus G-stem region implying that both perform similar functions even though they are from unrelated viruses. PMID: 24597516
    7. Authors show that D268, located in the segment consisting of residues 264 to 273, which refolds into postfusion helix F during G structural transition, is the major pH sensor while D274, D395, and D393 have additional contributions. PMID: 25210175
    8. Recombinant VSV with RABV-G drives strong expression of transgenes and spreads rapidly from neuron to neuron in only a retrograde manner. PMID: 23403489
    9. Energetic analyses revealed weakened interaction between Domain IV and the protein core at pH 5, which can be attributed to two pairs of structurally neighboring conserved and differentially protonated residues in the Domain IV-core interface. PMID: 22806964
    10. set of recombinant VSV particles bearing lethal mutations in G; study confirms hydrophobic fusion loops are critical for membrane fusion; underscores importance of the sequence elements surrounding the hydrophobic tips of fusion loops in driving fusion PMID: 21680501
    11. Data suggest that BMP preferentially affects the ability of VSV G to mediate lipid mixing during membrane fusion. PMID: 21333650
    12. adaptation of VSIV-6.8 to pHs 6.6 and 6.4 resulted in additional amino acid substitutions in areas of the glycoprotein that were not previously implicated in attachment or fusion. PMID: 15731252
    13. crystal structure; structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation PMID: 16840692
    14. structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G PMID: 17289996
    15. We now report that VSV glycoprotein G (gpG) is essential for the induction of a previously unrecognized CD14/TLR4-dependent response PMID: 17292937
    16. results suggest a new model of virus assembly in which an interaction of VSV nucleocapsids with G-protein-containing microdomains is a precursor to the formation of viral budding sites PMID: 18367537

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  • 亞細(xì)胞定位：
    Virion membrane; Single-pass type I membrane protein. Host membrane; Single-pass type I membrane protein. Note=The cytoplasmic domain sorts the protein to neurons dentrites instead of axons. When expressed in ex vivo polarized cells like epithelial cells, it sorts the protein to the basolateral side.
  • 蛋白家族：
    Vesiculovirus glycoprotein family
  • 數(shù)據(jù)庫鏈接：

    KEGG: vg:1489834



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