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Anti-Human Respiratory Syncytial Virus(RSV)(A2) Fusion Glycoprotein/RSV-F Monoclonal Antibody

Anti-Human Respiratory Syncytial Virus(RSV)(A2) Fusion Glycoprotein/RSV-F Monoclonal Antibody

SKU: E-AB-V1277-100

  • $ 35295


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Anti-Human Respiratory Syncytial Virus(RSV)(A2) Fusion Glycoprotein/RSV-F Monoclonal Antibody

 

SKU # E-AB-V1277
Reactivity RSV
Host Rabbit
Applications ELISA

 

Product Details

Isotype IgG
Host Rabbit
Reactivity RSV
Applications ELISA
Clonality Monoclonal
Immunogen Recombinant RSV (A2) Fusion glycoprotein / RSV-F Protein (His Tag)
Synonyms F, HRSVgp08
Concentration 1 mg/mL
Buffer 0.2 μm filtered solution in PBS.
Purification Method Protein A Affinity
Clone No. 302
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended.

 

Related Reagents

Applications Recommended Dilution
 ELISA 1:1000-10000

 

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. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. The G protein mediates attachment of the virus to cell surface receptors, while the F protein promotes fusion of the viral and cellular membranes, allowing entry of the virus ribonucleoprotein into the cell cytoplasm. The fusion (F) protein of RSV is synthesized as a nonfusogenic precursor protein (F), which during its migration to the cell surface is activated by cleavage into the disulfide-linked F1 and F2 subunits. This fusion is pH independent and occurs directly at the outer cell membrane, and the F2 subunit was identifed as the major determinant of RSV host cell specificity. The trimer of F1-F2 interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and induces the fusion between host cell and virion membranes. Notably, RSV fusion protein is unique in that it is able to interact directly with heparan sulfate and therefore is sufficient for virus infection. Furthermore, the fusion protein is also able to trigger p53-dependent apoptosis.