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- Ab03523-23.0 Anti-F protein [2E3]
- RSV
- Rabbit IgG
- Purified
- Ships in 5-6 weeks
- Ab03523-10.29 Anti-F protein [2E3]
- RSV
- Human Fab fragment
- His-Tagged
- Purified
- Ships in 5-6 weeks
Recombinant monoclonal antibody to F protein. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the phage display antibody 2E3.
UniProt Accession Number of Target Protein: P03420
Alternative Name(s) of Target: fusion glycoprotein; Fusion glycoprotein F0
Immunogen: A synthetic, fully human antibody library was used for panning against RSV prefusion and post fusion F proteins. The original antibody against RSV F protein was discovered following phage library panning and characterized.
Specificity: The original antibody is specific for prefusion F protein. The antibody binds the protein through a conformational epitope spanning across three distinct sections of the RSV F protein: residues 419–434, 443–448, and 459–467. F-protein plays a pivotal role in the pathogenesis of RSV by mediating the fusion between the viral and the host cell membrane. F protein exists in two distinct conformations: the metastable prefusion conformation and the stable post fusion conformation.
Application Notes: The specificity of the Fab and IgG1 format of the antibody was confirmed by ELISA analysis (EC50 value for IgG1 at 9.6 ng/mL). Surface plasmon resonance based studies demonstrated that the antibody bound exclusively to the prefusion conformation of the RSV F protein with an affinity Kd = 13 nM for monovalent Fab. The bivalent Fab exhibited neutralizing activities against both RSV A (Long) and B (Washington) strains with IC50 at 53.4 ng/mL and 515 ng/mL, respectively. The human IgG1 format showed an improved neutralizing activity against the RSV A strain (IC50 at 11.4 ng/mL) and comparable against the RSV B (Washington) strain (IC50 at 520 ng/mL).
Antibody first published in:
Chen et al. Discovery and Characterization of Phage Display-Derived Human Monoclonal Antibodies against RSV F Glycoprotein PLoS One. 2016; 11(6): e0156798. PMID:27258388
Note on publication:
The paper describes the generation and characterization of the antibody.