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COADS MSDS

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

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COADS MSDS
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RSF-V52H7-50ug
$465.00
In Stock - Delivery in 1-2 business days
RSF-V52H7-500ug
$3,170.00
In Stock - Delivery in 1-2 business days
RSF-V52H7
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Synonyms

Prefusion glycoprotein F0/pre-F protein (RSV)

Source

HRSV (A) Pre-fusion glycoprotein F0, His Tag (RSF-V52H7) is expressed from human 293 cells (HEK293).

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 when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Within the expressed region, several mutations were introduced to optimize the protein expression and stability.

The protein is designed as a trimer.

Endotoxin

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

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.
ACRO Quality Management System

Introduction de fond

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.