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Human respiratory syncytial virus (RSV) (A, rsb1734) glycoprotein G / RSV-G Protein (93% Homology) (His Tag)

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RSV RSV-G Protein Product Information
Protein Construction:A DNA sequence encoding the glycoprotein G extracellular domain (Asn 66-Arg297) of human respiratory syncytial virus A (93% homologous with strain rsb1734) (P27022-1) was expressed, with a C-terminal polyhistidine tag.
Expressed Host:Human Cells
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
RSV RSV-G Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Asn 66
Molecule Mass:The secreted recombinant human RSV-G comprises 242 amino acids and has a predicted molecular mass of 26.3 kDa. As a result of highly glycosylation, the apparent molecular mass of RSV protein G is approximately 60-90 kDa in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
RSV RSV-G Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Human RSV (A, rsb1734) glycoprotein G / RSV-G Protein (93% Homology) (His Tag) SDS-PAGE
Human RSV (A, rsb1734) glycoprotein G / RSV-G Protein (93% Homology) (His Tag) SDS-PAGE
Other RSV-G Recombinant Protein Products
RSV-G / Glycoprotein G Background

Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 80-90 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities.

RSV RSV-G / Glycoprotein G References
  • Martin-Gallardo A. et al., 1993, J Gen Virol. 74 : 453-8.
  • Jose AM. et al.,1997, J Gen Virol. 78: 2411-8.
  • Feldman SA. et al., 1999, J Virol. 73: 6610-7.
  • García-Beato R. et al., 2000, J Gen Virol. 81: 919-27.
  • Zlateva KT. et al., 2004, J Virol. 78: 4675-83.
  • Trento A. et al., 2006, J Virol. 80: 975-84.
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    Catalog: 11070-V08H2-10
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    All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.