RSV F Protein Extracellular Domain (Strain RSS-2) (recombinant)

Respiratory syncytial virus (RSV) fusion (F) protein is a surface glycoprotein encoded by the F gene in RSV RNA. It is synthesized as an inactive precursor protein, F0, that undergoes proteolytic cleavage to release the F1 and F2 subunits, which are joined together by two disulfide bonds. Mature RSV F protein is composed of an N-terminal fusion peptide (FP), two heptad repeats (HRs), a transmembrane domain, and a cytoplasmic tail and assembles into homotrimers on the virus surface. Upon insertion of the FP in the target cell membrane, the HRs form a six-helical bundle (6-HB) that enables RSV to fuse with the target cell. RSV F protein is highly conserved between RSV subtypes A and B with approximately 90% amino acid identities. RSV is the most common causative agent of pediatric lower respiratory tract infections. Cayman's RSV F Protein Extracellular Domain (Strain RSS-2) (recombinant) protein consists of 519 amino acids, has a calculated molecular weight of 57.8 kDa, and a predicted N-terminus of Phe22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the F0 and F1 proteins is approximately 63 and 44-53 kDa, respectively, due to glycosylation.Synonyms: Respiratory Syncytial Virus F Protein, Respiratory Syncytial Virus Fusion Protein, RSV Fusion Protein. Purity: >95% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Recombinant C-terminal His-tagged RSV F protein extracellular domain expressed in insect cells. Amino Acids: 22-529. MW: 57.8 kDa. Formulation: (Request formulation change), Lyophilized from sterile 20 mM Tris, pH 7.4, with 500 mM sodium chloride and 10% glycerol. UniProt Accession #: P03420.