Human metapneumovirus Post-fusion glycoprotein F0, His Tag (MALS verified)

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RSF-V52H5-100ug
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RSF-V52H5-1mg (500ug X 2)
$5,045.00
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RSF-V52H5
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Synonyms

Postfusion glycoprotein F0/post-F protein (HMPV)

Source

Human metapneumovirus Post-fusion glycoprotein F0, His Tag (RSF-V52H5) is expressed from human 293 cells (HEK293). It contains AA Leu 19- Thr 489 (Accession # Q6WB98).

Molecular Characterization

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

The protein has a calculated MW of 56.6 kDa. The protein migrates as 51-55 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

The protein is designed as a trimer.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in 0.1 M Sodium citrate, 0.5 M Arginine, pH5.5 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.

Shipping and Storage

This product is shipped at ambient temperature.

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:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

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.