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Ebola virus EBOV (subtype Bundibugyo, strain Uganda 2007) Glycoprotein / GP-RBD (Receptor Binding Domain) Protein (Fc Tag)

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EBOV EBOV-G Produktinformation zu Proteinen
Synonym:EBOV-GP
Proteinaufbau:A DNA sequence encoding the Bundibugyo ebolavirus(strain Uganda 2007) GP (ACI28624.1) (Met1-Val308) was expressed with the Fc region of human IgG1 at the C-terminus.
Spezies:EBOV
Expressionswirt:Human Cells
Form und Lieferung:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
EBOV EBOV-G Qualitätskontrollentests für Proteine
Reinheit:> 95 % as determined by SDS-PAGE
Endotoxin:< 1.0 EU per μg protein as determined by the LAL method.
Stabilität:Samples are stable for up to twelve months from date of receipt at -70℃
Prognostizierter N-Terminus:Ile 33
Molekülmasse:The recombinant Bundibugyo ebolavirus(strain Uganda 2007) GP consists 514 amino acids and predicts a molecular mass of 57.6 kDa.
Rezeptur:Lyophilized from sterile PBS, pH 7.4.
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
EBOV EBOV-G Leitfaden zur Nutzung von Proteinen
Lagerung:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Rekonstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EBOV-G Ähnliche Signalwege

    Other EBOV-G Recombinant Protein Products
    EBOV-G/Ebola Glycoprotein Hintergrund

    The fourth gene of the EBOV genome encodes a 160-kDa envelope-attached glycoprotein (GP) and a 110 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.

    EBOV EBOV-G/Ebola Glycoprotein Referenzen
    1. Volchkov VE, et al. Processing of the Ebola virus glycoprotein by the proprotein convertase furin. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5762-7.
    2. Lee JE, et al. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature. 2008 Jul 10;454(7201):177-82. doi: 10.1038/nature07082.
    3. Hood CL, et al. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity. J Virol. 2010 Mar;84(6):2972-82. doi: 10.1128/JVI.02151-09.
    4. Cook JD and Lee JE. The secret life of viral entry glycoproteins: moonlighting in immune evasion. PLoS Pathog. 2013 May;9(5):e1003258. doi: 10.1371/journal.ppat.1003258.
    5. Miller EH and Chandran K. Filovirus entry into cells - new insights. Curr Opin Virol. 2012 Apr;2(2):206-14. doi: 10.1016/j.coviro.2012.02.015.
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    Katalog: 40368-V02H-20
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    All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.
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