Recombinant RSV Post-fusion F-trimer Protein (strain A2)
Cat# DRA267-50ug
Size : 50ug
Brand : Novoprotein
Description Recombinant RSV (strain A2) Post-fusion F-trimer Protein is produced by our Mammalian expression system and the target gene encoding Gln26-Asn524( Phe137-Gly145 del) is expressed with a 8His tag at C-terminus.
Accession C3UPB8
Known As RSV F Protein; Respiratory syncytial virus Fusion glycoprotein;Post-fusion F
Mol Mass 55.4 kDa
APMol Mass 40-60&18-24 KDa, reducing conditions
Formulation Description Supplied as a 0.2 μm filtered solution of 40mM Tris-HCl, 500mM NaCl, 0.01% Tween20, pH7.4.
Purity-SDS-PAGE 
Greater than 95% as determined by reducing SDS-PAGE. (QC verified) Bioactivity-ELISA 
Immobilized Recombinant RSV Post-fusion F-trimer Protein (strain A2) (DRA267) at 5μg/ml (100 μl/well) can bind RSV F Antibody (4D5)(DA102). The ED50 of RSV F Antibody (4D5)(DA102) is 5.81 ng/ml. (Regularly tested) Storage - Reconstituted protein solution should be stored at ≤ -20°C.
- Stable for at least 24 months when stored as instructed.
Shipping The product is shipped on dry ice pack.Upon receipt, store it immediately at the temperature listed below.
Background Respiratory syncytial virus (RSV) is a highly contagious pathogen of the respiratory tract, primarily in infants and the elderly. A vaccine against RSV is currently not available, but is desired due to the high disease burden.RSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. The RSV fusion glycoprotein (RSV F) is an attractive vaccine antigen, since it is the principal target of RSV neutralizing antibodies in human sera. RSV F fuses the viral and host cell membranes by irreversible protein refolding from the labile prefusion conformation to the stable postfusion conformation. Like other class I fusion proteins, the inactive precursor, RSV F0, requires cleavage during intracellular maturation by a furin-like protease. RSV F contains two furin sites, which leads to three polypeptides: F2, p27 and F1, with the latter containing a hydrophobic fusion peptide at its N terminus. Neutralizing epitopes reside on both conformations, but those specific to pre-F are far more potent than those previously identified and present on post-F. The solution of the pre-F structure and its subsequent characterization and stabilization illustrates the value of a structure-based approach to vaccine development, and provides hope that a safe and effective RSV vaccine is possible.