Human RSV (B1) glycoprotein G / RSV-G Protein (His Tag)

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Human RSV (B1) glycoprotein G / RSV-G Protein (His Tag): Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Testing in progress
Protein Construction
A DNA sequence encoding the extracellular domain of human RSV strain B1 glycoprotein G (O36633-1) (His 67-Ala 299) was fused with a polyhistidine tag at the C-terminus and a signal peptide at the N-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
RSV
Predicted N Terminal
His 67
Molecule Mass
The secreted recombinant human RSV strain B1 glycoprotein G comprises 244 amino acids with a predicted molecular mass of 27 kDa. As a result of highly glycosylation, the apparent molecular mass of the recombinant protein is approximately 80-90 kDa in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile PBS, pH 7.4
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
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.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
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 (B1) glycoprotein G / RSV-G Protein (His Tag): Images

Human RSV (B1) glycoprotein G / RSV-G Protein (His Tag): Alternative Names

G Protein, RSV

RSV Glycoprotein G Background Information

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 8-9 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.
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.
  • Aptamers for respiratory syncytial virus detection
    Author
    Percze, K;Szakács, Z;Scholz, É;András, J;Szeitner, Z;Kieboom, CH;Ferwerda, G;Jonge, MI;Gyurcsányi, RE;Mészáros, T;
    Year
    2017
    Journal
    Sci Rep
    Application
    binding
  • Broadly reactive anti-RSV G antibodies from exposed individuals effectively inhibit infection of primary airway epithelial cells.
    Author
    Cortjens, B;Yasuda, E;Yu, X;Wagner, K;Claassen, YB;Bakker, AQ;van Woensel, JB;Beaumont, T;
    Year
    2017
    Journal
    J. Virol
    Application
    binding
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