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Anti-EBOV-G / Glycoprotein antibody

Cat.#: 101029

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Product Information

  • Product Name
    Anti-EBOV-G / Glycoprotein antibody
  • Documents
  • Description
    Rabbit polyclonal to EBOV-G / Glycoprotein
  • Tested applications
    ELISA, WB, IHC-P, IP
  • Species reactivity
    Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) GP-RBD / Glycoprotein
    Has cross-reactivity in WB with Ebola virus EBOV (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein / GP-RBD Protein (His Tag) (504337); Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) Glycoprotein / GP Protein (His Tag) (502529); Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP1 (mucin domain deleted) Protein (aa:Met1-Asp320, His Tag)(503320)
  • Immunogen
    EBOV EBOV-G / Glycoprotein (His Tag)
  • Isotype
    Rabbit IgG
  • Preparation
    Produced in rabbits immunized with purified, recombinant Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) GP-RBD / Glycoprotein (AAC54887.1; Met1-Phe308), and purified by antigen affinity chromatography.
  • Clonality
    Polyclonal
  • Formulation
    0.2 μm filtered solution in PBS
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    WB: 1-2 μg/ml

    ELISA: 0.1-0.2 μg/ml

    This antibody can be used at 0.1-0.2 μg/ml with the appropriate secondary reagents to detect Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) GP-RBD / Glycoprotein.

  • Validations

    Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) GP-RBD / Glycoprotein Antibody, Rabbit PAb, Antigen Affinity Purified, Western blot

    Ebola virus EBOV (subtype Zaire, strain Mayinga 1976) GP-RBD / Glycoprotein Antibody, Rabbit PAb, Antigen Affinity Purified, Western blot

  • 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.
  • References
    • 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.
    • 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.
    • 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.
    • 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.
    • 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.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"