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MABF2113-100UG
Sigma-AldrichAnti-EBOV GP Antibody, clone 1H3
Anti-EBOV GP clone 1H3, Cat. No. MABF2113, is a mouse monoclonal antibody that detects Ebola virus Envelope Glycoprotein and has been tested for use in ELISA and, Immunocytochemistry, Immunoprecipitation, and Neutralizing Applications.
More>>Anti-EBOV GP clone 1H3, Cat. No. MABF2113, is a mouse monoclonal antibody that detects Ebola virus Envelope Glycoprotein and has been tested for use in ELISA and, Immunocytochemistry, Immunoprecipitation, and Neutralizing Applications. Less<<
Envelope glycoprotein (UniProt: Q05320; also known as GP1,2; GP) is encoded by the GP gene (Gene ID: 911829) in Zaire Ebola virus. Ebola virus (EBOV) is a filovirus that is shown to cause severe viral hemorrhagic fever with high lethality. It has a single stranded, negative-sense RNA genome that encodes seven viral structural proteins including nucleoprotein, virion proteins, and glycoprotein. The glycoprotein is the most important protein involved in pathogenesis. It is a type I transmembrane surface protein shown to be responsible for receptor binding, viral entry, and cellular tropism. The GP gene is reported to undergo transcriptional editing to give rise to several glycosylated proteins, including the structural protein GP1,2, and the secreted non-structural glycoprotein (sGP). The GP is synthesized as a 676-amino acid polyprotein with a signal peptide (aa 1-32). This polyprotein is cleaved by the furin to yield two disulfide linked subunits known as GP1 (aa 33-501) and GP2 (aa 502-676), which together form the GP1,2 heterodimer. The GP1 acts as the receptor-binding subunit and GP2 as the membrane fusion subunit. The GP1 subunit is expressed on the cell surface with the C-terminus oriented toward the aqueous environment, while the N-terminus is bound to GP2 via disulfide bonds. The GP1 subunit contains the heavily glycosylated mucin-like domain (aa 305-485), which is responsible for its cytotoxic function. The glycoprotein contains two coiled coil regions (aa 554-595 and 615-634) that play a role in its oligomerization and fusion activity. Clone 1H3 recognizes the secreted glycoprotein form (sGP) and also recognizes glycoprotein lacking a large part of the mucin domain (GP1,2 Mucin333 458). It does not recognize VSV G/ZEBOVGP and subfragment D. When administered before virus challenge, it provides only a partial protection. (Ref.: Qiu, X., et al. (2011). Clin. Immunol. 141(2); 218-227).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG2a in PBS without azide.
Applications
Application
Anti-EBOV GP clone 1H3, Cat. No. MABF2113, is a mouse monoclonal antibody that detects Ebola virus Envelope Glycoprotein and has been tested for use in ELISA and, Immunocytochemistry, Immunoprecipitation, and Neutralizing Applications.
Key Applications
ELISA
Immunocytochemistry
Immunoprecipitation
Neutralization Assay
Application Notes
ELISA Analysis: A representative lot detected EBOV GP in ELISA applications (Qiu, X., et. al. (2011). Clin Immunol. 141(2):218-27).
Immunoprecipitation Analysis: Immunoprecipitation Analysis: A representative lot detected EBOV GP in Immunoprecipitation applications (Qiu, X., et. al. (2011). Clin Immunol. 141(2):218-27).
Immunocytochemistry Analysis: Immunocytochemistry Analysis: A representative lot detected EBOV GP in Immunocytochemistry applications (Qiu, X., et. al. (2011). Clin Immunol. 141(2):218-27).
Neutralizing Analysis: A representative provided partial protection when administered prior to virus challenge. (Qiu, X., et. al. (2011). Clin Immunol. 141(2):218-27).
ELISA Analysis: Various dilutions of this antibody detected Envelope glycoprotein in Recombinant Ebola virus Glycoprotein minus the transmembrane region (EBOV rGP TM).
Biological Information
Immunogen
Glycoprotein from Zaire Ebola virus, strain Mayinga, expressed in VSV G. Reverse genetics technique was used to create the recombinant virus VSV G/ZEBOV glycoprotein.
Clone
1H3
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 1H3 is a mouse monoclonal antibody that detects envelope glycoprotein of Zaire Ebola virus. It recognizes the secreted glycoprotein form (sGP) and binds to a conformational epitope in the first 295 amino acids.
Evaluated by ELISA with recombinant Ebola virus Glycoprotein minus the transmembrane region (EBOV rGP deltaTM).
ELISA Analysis: Various dilutions of this antibody detected EBOV GP in Recombinant Ebola virus Glycoprotein minus the transmembrane region (EBOV rGP deltaTM).
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Packaging Information
Material Size
100 μg
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Bestellnummer
GTIN
MABF2113-100UG
04054839755316
Documentation
Anti-EBOV GP Antibody, clone 1H3 Analysenzertifikate
Zaire ebolavirus (ZEBOV) can be transmitted by human-to-human contact and causes acute haemorrhagic fever with case fatality rates up to 90%. There are no effective therapeutic or prophylactic treatments available. The sole transmembrane glycoprotein (GP) is the key target for developing neutralizing antibodies. In this study, recombinant VSVΔG/ZEBOVGP was used to generate monoclonal antibodies (MAbs) against the ZEBOV GP. A total of 8 MAbs were produced using traditional hybridoma cell fusion technology, and then characterized by ELISA using ZEBOV VLPs, Western blotting, an immunofluorescence assay, and immunoprecipitation. All 8 MAbs worked in IFA and IP, suggesting that they are all conformational MAbs, however six of them recognized linearized epitopes by WB. ELISA results demonstrated that one MAb bound to a secreted GP (sGP 1-295aa); three bind to a part of the mucin domain (333-458aa); three MAbs recognized epitopes on the C-terminal domain of GP1 (296-501aa); and one bound to full length GP (VLPs/GP1,2 ΔTm). Using a mouse model these MAbs were evaluated for their therapeutic capacity during a lethal infection. All 8 MAb improved survival rates by 33%-100% against a high dose lethal challenge with mouse-adapted ZEBOV. This work has important implications for further development of vaccines and immunotherapies for ZEBOV infection.
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