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HRSV (A) Pre-fusion glycoprotein F0, His Tag (MALS verified)

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  • Source
    HRSV (A) Fusion glycoprotein F0, His Tag (RSF-V52H7) is expressed from human 293 cells (HEK293).
    Predicted N-terminus: Gln 26
  • Molecular Characterization

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 56.1 kDa. The protein migrates as 60-65 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.

    >90% as determined by SEC-MALS.

  • Formulation

    Supplied as 0.2 μm filtered solution in 0.1 M Sodium citrate, 150 mM NaCl, pH5.5 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
SDS-PAGE
Prefusion glycoprotein F0/pre-F protein (RSV) SDS-PAGE

HRSV (A) Pre-fusion glycoprotein F0, 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%.

SEC-MALS
Prefusion glycoprotein F0/pre-F protein (RSV) MALS images

The purity of HRSV (A) Pre-fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H7) is more than 90% and the molecular weight of this protein is around 175-200 kDa verified by SEC-MALS.

Bioactivity-ELISA
 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized HRSV (A) Fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H7) at 2 μg/mL (100 μL/well) can bind Anti-Fusion glycoprotein F0 Antibody, Human IgG1 (D25) with a linear range of 0.2-1 ng/mL (QC tested).

 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized HRSV (A) Pre-fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H7) at 1 μg/mL (100 μL/well) on an Nickel Coated plate can bind Monoclonal Anti-HRSV F Antibody, Human IgG1 (AM14) with a linear range of 0.2-2 ng/mL (QC tested).

 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized HRSV (A) Pre-fusion glycoprotein F0, His Tag (MALS verified) (Cat. No. RSF-V52H7) at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-RSV-F0 broadly Antibody, Mouse IgG1 (3B4) with a linear range of 0.098-3.125 ng/mL (Routinely tested).

 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized HRSV (A) Pre-fusion glycoprotein F0, His Tag (MALS verified) (Cat. No. RSF-V52H7) at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-RSV-F0 broadly Antibody, Mouse IgG1 (4G2) with a linear range of 0.024-0.781 ng/mL (Routinely tested).

 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized HRSV (A) Fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H7) at 2 μg/mL (100 μL/well) can bind Anti-Fusion glycoprotein F0 Antibody, Mouse IgG2a (101F) with a linear range of 0.2-5 ng/mL (Routinely tested).

 Prefusion glycoprotein F0/pre-F protein (RSV) ELISA

Immobilized Anti-Fusion glycoprotein F0 Antibody, Mouse IgG2a (101F) at 2 μg/mL (100 μL/well) can bind HRSV (A) Fusion glycoprotein F0, His Tag (Cat. No. RSF-V52H7) with a linear range of 0.1-13 ng/mL (Routinely tested).

  • 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. The RSV fusion glycoprotein (RSV F) is the principal target of RSV neutralizing antibodies in human sera. The RSV F is a type I viral fusion protein synthesized as inactive, single-chain polypeptides that assemble into trimers. RSV F fuses the viral and host cell membranes by irreversible protein refolding from the labile prefusion conformation to the stable post-fusion conformation. Both states exhibit epitopes targeted by neutralizing antibodies, and post-fusion RSV F is being developed as a vaccine candidate.
  • Clinical and Translational Updates

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