Recombinant Human Respiratory Syncytial Virus B Fusion Glycoprotein F0 (F) Protein (His)

Name: Recombinant Human Respiratory Syncytial Virus B Fusion Glycoprotein F0 (F) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09334P
Price: 460.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Featured viral antigens molecules, Other viral antigens, Recombinant proteins, Viral antigen

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Product Overview

Description	Recombinant Human Respiratory Syncytial Virus B Fusion Glycoprotein F0 (F) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O36634
Target Symbol	F
Synonyms	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)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	FLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVSLSNGVSVLTSKVLDLKNYINNQLLPIVNQQSCRISNIETVIEFQQKNSRLLEINREFSVNAGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYVVQLPIYGVIDTPCWKLHTSPLCTTNIKEGSNICLTRTDRGWYCDNAGSVSFFPQADTCKVQSNRVFCDTMNSLTLPSEVSLCNTDIFNSKYDCKIMTSKTDISSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKNLYVKGEPIINYYDPLVFPSDEFDASISQVNEKINQSLAFIRRSDELLHNVNTGKSTTNIMITTIIIVIIVVLLSLIAIGLLLYCKAKNTPVTLSKDQLSGINNIAFSK
Expression Range	137-574aa
Protein Length	Partial
Mol. Weight	50.1 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
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 References	KEGG: vg:1489825

Gene Functions References

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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.