Product Details

Purity

Greater than 90% as determined by SDS-PAGE.

Target Names

Uniprot No.

O36634

Research Area

Others

Alternative Names

FFusion glycoprotein F0; Protein F) [Cleaved into: Fusion glycoprotein F2'; Interchain peptide; Fusion glycoprotein F2; Fusion glycoprotein F1]

Species

Human respiratory syncytial virus B (strain B1)

Source

Yeast

Expression Region

137-574aa

Target Protein Sequence

FLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYINNQLLPIVNQQSCRISNIETVIEFQQKNSRLLEINREFSVNAGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYVVQLPIYGVIDTPCWKLHTSPLCTTNIKEGSNICLTRTDRGWYCDNAGSVSFFPQADTCKVQSNRVFCDTMNSLTLPSEVSLCNTDIFNSKYDCKIMTSKTDISSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKNLYVKGEPIINYYDPLVFPSDEFDASISQVNEKINQSLAFIRRSDELLHNVNTGKSTTNIMITTIIIVIIVVLLSLIAIGLLLYCKAKNTPVTLSKDQLSGINNIAFSK
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.

Mol. Weight

50.1 kDa

Protein Length

Partial

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Target Background

Function

Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.; Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the coiled coil regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein may trigger p53-dependent apoptosis.; Major determinant of the species specificity of RSV infection. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate. F protein is involved in the entry into the host cell through the interaction with host IGFR1. This interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell surface where it can bind fusion glycoprotein F1. Later in infection, F protein expressed at the plasma membrane of infected cells can mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. F protein seems to trigger p53-dependent apoptosis.

Gene References into Functions

used a rHPIV1 vector, bearing a stabilized attenuating mutation, to express the RSV F glycoprotein bearing amino acid substitutions that increase its stability in the pre-F form, the most immunogenic form that elicits highly functional virus-neutralizing antibodies PMID: 28835504
Data suggest that the profile of IgG3 specific to fusion protein (F protein) reflects infants' own antibody response after respiratory syncytial virus (RSV) infection. PMID: 28111238
Prefusion RSV F induced a larger quantity and higher quality of RSV-neutralizing serum antibodies and was highly protective PMID: 26157122
Authors defined residues 79/191 as critical for human respiratory syncytial virus strain A2-line 19 F fusion activity and 357/371 as playing a role in mucus induction. PMID: 25339762
R145 epitope is required for the post-fusion conformation change of F protein. PMID: 25010277
A K66E mutation in the F2 fragment of the fusion (F) protein as the cause of the growth and CPE differences. PMID: 24092758
Data indicate that despite the conserved nature of the fusion protein (F protein), the variation does occur between different strains and between the subtypes. PMID: 23734183
RAGE appeared to interact directly with the F protein, but, rather than inhibiting respiratory syncytial virus entry into host cells, virus replication and budding, membrane-expressed RAGE or soluble RAGE blocked F-protein-mediated syncytium formation and sloughing. PMID: 23559480
Mutation Val533Met and Asn268Ile in the transmembrane domain of the F protein are criticle for immune escape. PMID: 22411099
Developed a new method that combines sucrose gradient ultracentrifugation and a two-step chromatographic process, to purify RSV F from RSV particles propagated in HEp-2 cells. PMID: 21979254
The present study demonstrates the silencing of the HRSV F gene using siRNA. PMID: 19507066
conformational changes that follow activation of HRSV F by proteolytic cleavage require a functional fusion peptide PMID: 16690930
cysteine residues in extracellular domain contribute to protein folding and transport to cell surface PMID: 16723026
metastable state converted in vitro to more stable, fusogenic sex-helix bundle conformation by increase in thermal energy PMID: 19922971

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Subcellular Location

[Fusion glycoprotein F0]: Host Golgi apparatus membrane; Single-pass membrane protein.; [Fusion glycoprotein F1]: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.; [Fusion glycoprotein F2]: Virion membrane. Host cell membrane.

Protein Families

Paramyxoviruses fusion glycoprotein family

Database Links

KEGG: vg:1489825

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Code	CSB-YP516611HXK
Size	$250
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human respiRatory syncytial virus B Fusion glycoprotein F0 (F), partial

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