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Your Position: > Protein > Glycoprotein G / G > RSG-V5221

HRSV (A) Glycoprotein G Protein, His Tag

  • Synonym
    Glycoprotein G,G,mG,Attachment glycoprotein G,Membrane-bound glycoprotein
  • Source
    HRSV (A) Glycoprotein G Protein, His Tag(RSG-V5221) is expressed from human 293 cells (HEK293). It contains AA His 67 - Arg 297 (Accession # P20895).
    Predicted N-terminus: His 67
  • Molecular Characterization
    Glycoprotein G / G Structure

    This protein carries a polyhistidine tag at the C-terminus

    The protein has a calculated MW of 27.0 kDa. The protein migrates as 46-90 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Glycoprotein G / G SDS-PAGE

HRSV (A) Glycoprotein G Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

  • 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.
  • Clinical and Translational Updates

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