Anti-Henipavirus (Clone: HENV-103)
Antibody Isotype:
Human IgG1
Antibody Clonality:
Monoclonal
Applications:- Flow Cytometry
- Neutralisation
Storage:
Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one year. For longer term storage aseptically aliquot in working volumes without diluting and store at ? -70°C. Avoid Repeated Freeze Thaw Cycles.
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This product comes from:
US.
Typical lead time:
14-21 working days.
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Further Information
Henipavirus RBP is an envelope glycoprotein.
? 5.0 mg/ml
Purified No Carrier Protein
This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Sequenced from human samples with prior exposure to equine Hendra virus (HeV) vaccine, targeting distinct antigenic sites.
Henipavirus spp. are enveloped, single-stranded RNA viruses in the family Paramyxovirus1. Five species have been identified, two of which, Hendra virus (HeV) and Nipah virus (NiV), are highly virulent emerging pathogens with high case-fatality ratios. The other three species, Cedar virus, Ghanaian bat virus, and Mojiang virus are not known to cause human disease. Pteropid bats are the reservoir host. HeV is transmitted by direct contact with infected horses, their fluids, or tissues1. Horses are infected by exposure to pteropid bats. NiV is transmitted by contact with infected pigs or bats and person-to-person. Both HeV and NiV cause severe influenza-like illness that can progress to encephalitis.
Potently neutralizing antibodies to HeV and/or NiV have been identified2, 3, 4, 5. HENV-103 was isolated from circulating B cells of an individual exposed to equine HeV vaccine5. Peripheral blood mononuclear cells were tested for binding to recombinant forms of the receptor binding protein (RBP) of NiVB, NiVM, or HeV. The mAb panel grouped into at least six distinct antigenic sites, A-F. HENV-103, group D, binds recombinant RBP and neutralizes HeV, NiVM, and NiVB.. HENV-103 maps to a distinct site on the HeV-RPB head domain spanning the β1 and β6 propeller blades, a region at the interface between protomers within the dimer-of-dimers structure of the HeV-RBP tetramer, suggesting a semi-cryptic site of vulnerability. nsEM mapping shows that HENV-103 binds at the putative dimeric interface. Binding of HENV-103 to RBP is enhanced by ephrin-B2.
?95% monomer by analytical SEC
Henipavirus
