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Description
HRSVA (strain A2) pre-fusion glycoProtein F0 His Tag ProteinProduct Specification Synonyms Prefusion glycoprotein F0 pre F protein (RSV) Accession ACO83301. 1 Amino Acid Sequence Gln26 Leu513 with His Tag at the C Terminus. Some mutations are introduced to stabilize the trimeric prefusion state of RSV Fusion glycoprotein. Expression System HEK293 Molecular Weight 55 72kDa (Reducing) Purity 90% by SDS PAGE Conjugation Unconjugated Tag His Tag Physical Appearance Liquid Storage Buffer PBS, PH7. 4 Reference
Product Specification
| Synonyms | Prefusion glycoprotein F0/pre-F protein (RSV) |
| Accession | ACO83301.1 |
| Amino Acid Sequence | Gln26-Leu513 with His Tag at the C-Terminus. Some mutations are introduced to stabilize the trimeric prefusion state of RSV Fusion glycoprotein. |
| Expression System | HEK293 |
| Molecular Weight | 55-72kDa (Reducing) |
| Purity | ＞90% by SDS-PAGE |
| Conjugation | Unconjugated |
| Tag | His Tag |
| Physical Appearance | Liquid |
| Storage Buffer | PBS, PH7.4 |
| Reference | Capella C, Chaiwatpongsakorn S, Gorrell E, Risch ZA, Ye F, Mertz SE, Johnson SM, Moore-Clingenpeel M, Ramilo O, Mejias A, Peeples ME. Prefusion F, Postfusion F, G Antibodies, and Disease Severity in Infants and Young Children With Acute Respiratory Syncytial Virus Infection. J Infect Dis. 2017 Dec 12;216(11):1398-1406. |
Background
Human respiratory syncytial virus (HRSV) is the predominant etiological agent of acute lower respiratory tract infections in infants and demonstrates capacity for recurrent infections throughout life. The RSV fusion glycoprotein (RSV F) serves as the primary target for neutralizing antibodies in human sera. As a class I viral fusion protein, RSV F is synthesized as an inactive single-chain polypeptide that undergoes trimeric assembly.Membrane fusion is mediated through an irreversible conformational rearrangement from a metastable prefusion state to a stable postfusion conformation. Both structural states present distinct epitopes recognized by neutralizing antibodies. Notably, the postfusion RSV F conformation is currently under development as a promising vaccine candidate due to its structural stability and immunogenic properties
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