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.
With over a decade of experience in phage display technology, Creative Biolabs can provide a series of antibody or peptide libraries that are available for licensing or direct screening. These ready-to-use libraries are invaluable resources for isolating target-specific binders for various research, diagnostic or therapeutic applications.
Creative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
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Recombinant Humanized (from mouse) Antibody specifically binds to RSV, expressed in Chinese Hamster Ovary cells(CHO)
Target
RSV
Type
Humanized (from mouse) 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 WB, IF, IP, Neut, FuncS, ELISA, FC and most other immunological methods.
Specific Activity
Tested positive against native antigen.
Protein Construction
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: QVQLVQS; L Chain: DIQMTQS
Purity
Purity >95% by SDS-PAGE.
Storage
Store at -20°C. Avoid multiple freeze/thaw cycles.
BACKGROUND
Introduction
Humanized Anti-Human RSV Monoclonal Antibody binds to the fusion glycoprotein of RSV. This prevents its binding and uptake by host cellular receptors. This product has the same active ingredient as Palivizumab.
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. 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.