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EBOV-G/Ebola Glycoprotein Rabbit MAb

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    EBOV EBOV-G Antibody Product Information
    Immunogen:Recombinant Sudan ebolavirus EBOV-G / Glycoprotein Protein (Catalog#40094-V08H)
    Clone ID:106
    Ig Type:Rabbit IgG
    Concentration:
    Endotoxin:
    Formulation:0.2 μm filtered solution in PBS
    Preparation:This antibody was obtained from a rabbit immunized with purified, recombinant Sudan ebolavirus Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP1 (mucin domain deleted) (rSudan ebolavirus Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP1 (mucin domain deleted); Catalog#40094-V08H; Q7T9D9; Met1-Asp320).
    Other EBOV-G Antibody Products

    Anti-Histone H3 rabbit monoclonal antibody at 1:200 dilution

    Lane A: NIH3T3 Whole Cell Lysate

    Lane B: Hela Whole Cell Lysate

    Lysates/proteins at 30 μg per lane.

    Secondary

    Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution.

    Developed using the ECL technique.

    Performed under reducing conditions.

    Predicted band size:15 kDa

    Observed band size:17 kDa

    EBOV-G/Ebola Glycoprotein Background

    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 References
    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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    Catalog: 40094-R106-50
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    Datasheet & Documentation

    All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.
    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"