Rabbit anti-Ebola virus EBOV Glycoprotein/GP1 Monoclonal Antibody | anti-EBOV-G antibody

Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein/GP1 (mucin domain deleted) Antibody, Rabbit MAb

Cat. Num. AAA8110603

• Reactivity: Ebola virus
• Applications: Western Blot, ELISA
• Purity: Protein A
• Synonyms: EBOV Glycoprotein/GP1; Monoclonal Antibody; Ebola virus EBOV (Subtype Sudan; strain Gulu) Glycoprotein/GP1 (mucin domain deleted) Antibody; Rabbit MAb; anti-EBOV-G antibody

• Host: Rabbit
• Reactivity: Ebola virus
• Clonality: Monoclonal
• Isotype: Rabbit IgG
• Clone Number: 106
• Specificity: Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein/GP1 (mucin domain deleted)
• Purity/Purification: Protein A
• Form/Format: Liquid; 0.2um filtered solution in PBS

• Applicable Applications for anti-EBOV-G antibody: Western Blot (WB), ELISA (EIA)
• Application Notes: WB: 1:1000-1:5000; ELISA: 1:5000-1:10,000; Antibody's applications haven't been validated with corresponding virus positive samples.
• Immunogen: Recombinant Sudan ebolavirus EBOV-G/Glycoprotein Protein
• Conjugation: Unconjugated
• 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)).
• Preparation and Storage: This antibody can be stored at 2-8 degree C for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20 degree C to -80 degree C. Preservative-Free. Avoid repeated freeze-thaw cycles.

Western Blot (WB)

(Anti-Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP Protein (aa:Met1-Asn637) rabbit monoclonal antibody at 1:1000Sample:Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein / GP Protein (aa:Met1-Asn637)Lane A: 20ngLane B: 5ngSecondaryGoat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique. Performed under reducing conditions.)

Related Product Information for anti-EBOV-G antibody

The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 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, beta-integrins, folate receptor-alpha, 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.

NCBI and Uniprot Product Information

• NCBI GI #: 75559166
• NCBI GeneID: 3160774
• UniProt Accession #: Q7T9D9
• NCBI Official Full Name: Envelope glycoprotein
• NCBI Official Symbol: GP
• NCBI Protein Information: spike glycoprotein; small secreted glycoprotein; second secreted glycoprotein
• UniProt Protein Name: Envelope glycoprotein
• UniProt Gene Name: GP
• UniProt Synonym Gene Names: GP

Uniprot Description

GP1 is responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection). Binding to the macrophage specific lectin CLEC10A also seem to enhance virus infectivity. Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection. Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably induces a conformational change of GP2, allowing its binding to the host entry receptor NPC1 and unmasking its fusion peptide to initiate membranes fusion.