Recombinant RSV-F Post Fusion
Data
![SDS PAGE RSV-F Leinco Prod No R602](https://www.leinco.com/wp-content/uploads/2024/03/SDS-PAGE-R602.jpg)
NR: 5µg non-reduced Recombinant RSV-F post fusion protein, (Leinco Prod. No.: R602)
![Direct Binding of RSV-F Leinco Prod No. R602](https://www.leinco.com/wp-content/uploads/2024/03/directBinding-RSV-F-R602.jpg)
Binding was measured by ELISA. RSV-F (Leinco Prod. No.: R602) was immobilized at 1 µg/mL. Anti-RSV-F antibody (Leinco Prod. No.: LT558) was titrated.
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BackgroundRespiratory syncytial virus (RSV) is a major cause of acute lower respiratory tract infection and hospitalization in infants1. RSV F protein is a type I integral membrane protein essential for viral membrane fusion that is highly conserved among isolates of RSV A and B subgroups and is the primary target for RSV antiviral drug development2. RSV F protein is synthesized as a 574 amino acid inactive precursor, assembled into a trimer, post-translationally modified, and then cleaved during activation for membrane fusion to produce F1, F2, and intervening peptide pep272. When functional F protein trimer in the virion membrane is triggered, F protein merges virus and host-cell membranes using the difference in folding energy between its pre-fusion (pre-F) and post-fusion (post-F) forms3. During infection, RSV-neutralizing antibodies target epitopes that reside primarily on the pre-F conformation3, 4, particularly antigenic site Ø on the apex of pre-F, which is highly sensitive to neutralization and exclusive to the pre-F conformation5. However, some neutralizing sites are common between pre- and post-F, including Site II, which binds the antibodies Motavizumab, Palivizumab, and 47F, as well as Site IV which binds 101F6. Additionally, the RSV F post-fusion trimer elicits high titers of neutralizing antibody when administered to mice and cotton rats7. Both pre- and post-F protein conformations are targets of RSV vaccine development8.
Recombinant RSV-F Post Fusion Protein is provided under an intellectual property license from the National Institutes of Health (NIH). The purchase of this protein conveys to the buyer the non-transferable right to use the purchased protein for research use only (RUO). As this protein is protected by the intellectual property rights of the NIH, the buyer of this protein (academic or commercial) is expressly prohibited from using the protein or any derivative in any commercial (revenue generating) activity. Such activities may include, but are not limited to, manufacturing, services, therapeutics, diagnostics, prophylactics or resale (including RUO). Protein DetailsSpecies Viral Format Purified No Carrier Protein Purity ≥95% by SDS Page Endotoxin Level ≤ 1.0 EU/mg as determined by the LAL method Protein Accession No. P03420 State of Matter Lyophilized SDS-Page Molecular Weight ~180k Non-reducing conditions Predicted Molecular Mass 60.5k monomer 181.5k Trimer Formulation Lyophilized from PBS + 5% Trehalose Reconstitution Reconstitute at 0.1-1 mg/ml using filtered deionized water. Gently mix by vortexing and/or inversion until fully dissolved. Centrifuge if necessary. Storage and Stability This lyophilized protein is stable for twelve months when stored at -20°C to -70°C. After aseptic reconstitution, this protein may be stored for one month at 2°C to 8°C or for three months at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. Country of Origin USA Shipping Ambient Species Viral Regulatory Status Research Use Only NCBI Gene Bank Applications and Recommended Usage ? (Quality Tested by Leinco) ELISA, SDS-PAGE, WB References & Citations1. Hammitt LL, Dagan R, Yuan Y, et al. N Engl J Med. 386(9):837-846. 2022.
2. McLellan JS, Ray WC, Peeples ME. Curr Top Microbiol Immunol. 372:383-104. 2013. 3. McLellan JS, Chen M, Joyce MG, et al. Science. 342(6158):592-598. 2013. 4. Magro M, Mas V, Chappell K, et al. Proc Natl Acad Sci U S A. 109(8):3089-3094. 2012. 5. Crank MC, Ruckwardt TJ, Chen M, et al. Science. 365(6452):505-509. 2019. 6. Steff AM, Monroe J, Friedrich K, et al. Nat Commun. 8(1):1085. 2017. 7. Swanson KA, Settembre EC, Shaw CA, et al. Proc Natl Acad Sci U S A. 108(23):9619-9624. 2011. 8. Graham BS, Modjarrad K, McLellan JS. Curr Opin Immunol. 35:30-38. 2015. 9. Espeseth AS, Cejas PJ, Citron MP, et al. NPJ Vaccines. 5(1):16. 2020. Technical ProtocolsCertificate of AnalysisIMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein. |
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