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Recombinant monoclonal antibody to Human RSV. Palivizumab is a monoclonal antibody produced by recombinant DNA technology. It is used in the prevention of respiratory syncytial virus (RSV) infections. It is recommended for infants that are high-risk because of prematurity or other medical problems such as congenital heart disease. Palivizumab is a humanized monoclonal antibody (IgG) directed against an epitope in the A antigenic site of the F protein of RSV.
IgG1 - kappa
The details of the immunogen for this antibody are not available.
Suitable for use in IF, IP, Neut, FuncS, ELISA, FC, WB and most other immunological methods.
Tested positive against native RSV antigen
Immunoglobulin G1,anti-(respiratory syncytial virus protein F) (human-mouse monoclonal 493 gamma 1-chain),disulfide with human-mouse monoclonal 493 kappa-chain,dimer
Predicted N terminal
H chain: QVQLVQSL chain: DIQMTQS
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Store it under sterile conditions at -20°C upon receiving. Recommend to pack the protein into smaller quantities for optimal storage.
Humanized Anti-Human RSV Monoclonal Antibody binds to the fusion glycoprotein of RSV. This prevents its binding and uptake by host cellular receptors.
Respiratory Syncytial Virus (RSV) Fusion (F) Glycoprotein is a Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis.