Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
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Recombinant humanized (from mouse) antibody expressed in CHO binding to RSV glycoprotein F. Motavizumab is a humanized monoclonal antibody for the prevention of respiratory syncytial virus infection in high-risk infants.
Target
RSV glycoprotein F
Type
IgG1 - kappa
Immunogen
The details of the immunogen for this antibody are not available.
Species Reactivity
RSV
Expression Host
CHO
Applications
Suitable for use in IF, IP, Neut, FuncS, ELISA, FC, WB and most other immunological methods.
CAS
677010-34-3
Trade name
numax
Predicted N terminal
QVTLRESG
Molecular Weight
Approximately 148 kDa
Purity
>95.0% as determined by analysis by RP-HPLC.
Size
1mg
Storage
4°C. For long term storage, aliquot and store at -20°C. Repeated thawing and freezing must be avoided.
BACKGROUND
Introduction
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.
Antigen Description
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.
Keywords
F antibody Fusion glycoprotein F0;Protein F; RSV Fusion (F) Glycoprotein