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Recombinant HRSV (A) glycoprotein G  pdf  pdf  pdf


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Synonym

RSV-G, G, mG

Source

Recombinant Human RSV (A) glycoprotein G /RSV-G Protein (rh RSV-G) His 67 - Arg 297 (Accession # P20895) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

rh RSV-G is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 26.2 kDa. The predicted N-terminus is His 67. DTT-reduced Protein migrates as 60-94 kDa in SDS-PAGE due to glycosylation.

Endotoxin

Less than 1.0 EU per μg of the rh RSV-G by the LAL method.

Purity

>90% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

Contact us for customized product form or formulation.

Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

 

SDS-PAGE


Recombinant Human RSV (A) glycoprotein G /RSV-G Protein
The purity of rh RSV-G was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 

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. Human respiratory syncytial virus A (strain Long) major surface glycoprotein G (RSV-G), a member of the pneumoviruses glycoprotein G family, is also known as attachment glycoprotein G and membrane-bound glycoprotein (mG), which contains a linear heparin binding domain essential for virus attachment to the host. Concretely speaking, RSV-G can attache the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Furthermore, RSV-G can also interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, RSV-G lacks both neuraminidase and hemagglutinating activities.

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References

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