Summary
| Production Name | Anti-HeV/NiV Glycoprotein G Antibody |
| Description | Recombinant human monoclonal antibody |
| Host | Human |
| Application | ELISA, Neutralization |
| Reactivity | Hendra virus (isolate Horse/Autralia/Hendra/1994) & Nipah virus |
Performance
| Conjugation | Unconjugated |
| Modification | Unmodified |
| Isotype | IgG1, kappa |
| Clonality | Monoclonal |
| Form | Liquid |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Buffer | 0.01M PBS, pH 7.4. |
| Purification | Protein A/G purified from cell culture supernatant. |
Immunogen
| Gene Name | Glycoprotein G |
| Alternative Names | G, Glycoprotein G, Attachment glycoprotein, Receptor binding protein, RBP |
| Gene ID | |
| SwissProt ID | O89343, Q9IH62 |
Application
| Dilution Ratio | ELISA 1:5000-1:20000 |
| Molecular Weight |
Background
Nipah virus (NiV), a highly pathogenic zoonotic paramyxovirus, mediates host cell entry through the coordinated action of two envelope glycoproteins: the attachment glycoprotein (G), which engages the host cell receptors ephrin-B2 and ephrin-B3, and the fusion glycoprotein (F), which drives membrane fusion following receptor binding. These viral surface proteins, along with the viral RNA-dependent RNA polymerase (RdRp) complex comprising the nucleoprotein (N), phosphoprotein (P), and large polymerase protein (L), constitute the primary molecular targets for therapeutic intervention and vaccine development. The conserved receptor-binding interface of the G protein and the fusion machinery of the F protein represent particularly attractive targets for neutralizing antibodies and entry inhibitors, while the viral replication machinery offers potential targets for broad-spectrum antiviral compounds targeting paramyxovirus transcription and replication.
Research Area
Microbiology&Infectious Disease