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SDS-PAGE

Fusion glycoprotein F0 (F) Recombinant Protein | F recombinant protein

Recombinant Human respiratory syncytial virus A Fusion glycoprotein F0 (F), partial

Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Fusion glycoprotein F0 (F); Recombinant Human respiratory syncytial virus A Fusion glycoprotein F0 (F); partial; F recombinant protein
Ordering
For Research Use Only!
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE.
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Sequence Positions
27-529aa; Full Length of Mature Protein
Sequence
NITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITT
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

SDS-PAGE
Related Product Information for F recombinant protein
During virus entry, induces fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. The fusogenic activity is inactive untill entry into host cell endosome, where a furin-like protease cleaves off a small peptide between F1 and F2. Interacts directly with heparan sulfate and may participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F 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. The fusion protein is also able to trigger p53-dependent apoptosis.
References
Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus.Collins P.L., Huang Y.T., Wertz G.W.Proc. Natl. Acad. Sci. U.S.A. 81:7683-7687(1984) Nucleotide sequence analysis of the respiratory syncytial virus subgroup A cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated virus vaccine candidate.Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.Virology 225:419-422(1996) Acquisition of the ts phenotype by a chemically mutagenized cold-passaged human respiratory syncytial virus vaccine candidate results from the acquisition of a single mutation in the polymerase (L) gene.Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.Virus Genes 13:269-273(1996) A cold-passaged, attenuated strain of human respiratory syncytial virus contains mutations in the F and L genes.Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.Virology 208:478-484(1995) Recombinant respiratory syncytial virus (RSV) bearing a set of mutations from cold-passaged RSV is attenuated in chimpanzees.Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.J. Virol. 72:4467-4471(1998) Fatty acid acylation of the fusion glycoprotein of human respiratory syncytial virus.Arumugham R.G., Seid R.C. Jr., Doyle S., Hildreth S.W., Paradisio P.R.J. Biol. Chem. 264:10339-10342(1989) RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation.Pastey M.K., Crowe J.E. Jr., Graham B.S.J. Virol. 73:7262-7270(1999) The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate.Feldman S.A., Audet S., Beeler J.A.J. Virol. 74:6442-6447(2000) The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil.Matthews J.M., Young T.F., Tucker S.P., Mackay J.P.J. Virol. 74:5911-5920(2000) Furin cleavage of the respiratory syncytial virus fusion protein is not a requirement for its transport to the surface of virus-infected cells.Sugrue R.J., Brown C., Brown G., Aitken J., McL Rixon H.W.J. Gen. Virol. 82:1375-1386(2001) Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion.Gonzalez-Reyes L., Ruiz-Argueello M.B., Garcia-Barreno B., Calder L., Lopez J.A., Albar J.P., Skehel J.J., Wiley D.C., Melero J.A.Proc. Natl. Acad. Sci. U.S.A. 98:9859-9864(2001) Respiratory syncytial virus (RSV) fusion protein subunit F2, not attachment protein G, determines the specificity of RSV infection.Schlender J., Zimmer G., Herrler G., Conzelmann K.K.J. Virol. 77:4609-4616(2003) The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasma membrane sorting sequence.Brock S.C., Heck J.M., McGraw P.A., Crowe J.E. Jr.J. Virol. 79:12528-12535(2005) The fusion protein of respiratory syncytial virus triggers p53-dependent apoptosis.Eckardt-Michel J., Lorek M., Baxmann D., Grunwald T., Keil G.M., Zimmer G.J. Virol. 82:3236-3249(2008) The RSV F and G glycoproteins interact to form a complex on the surface of infected cells.Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.Biochem. Biophys. Res. Commun. 366:308-313(2008) Host cell entry of respiratory syncytial virus involves macropinocytosis followed by proteolytic activation of the F protein.Krzyzaniak M.A., Zumstein M.T., Gerez J.A., Picotti P., Helenius A.PLoS Pathog. 9:E1003309-E1003309(2013) Structural basis of respiratory syncytial virus neutralization by motavizumab.McLellan J.S., Chen M., Kim A., Yang Y., Graham B.S., Kwong P.D.Nat. Struct. Mol. Biol. 17:248-250(2010) Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion protein.Roymans D., De Bondt H.L., Arnoult E., Geluykens P., Gevers T., Van Ginderen M., Verheyen N., Kim H., Willebrords R., Bonfanti J.F., Bruinzeel W., Cummings M.D., van Vlijmen H., Andries K.Proc. Natl. Acad. Sci. U.S.A. 107:308-313(2010) Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes.McLellan J.S., Yang Y., Graham B.S., Kwong P.D.J. Virol. 85:7788-7796(2011) Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers.Swanson K.A., Settembre E.C., Shaw C.A., Dey A.K., Rappuoli R., Mandl C.W., Dormitzer P.R., Carfi A.Proc. Natl. Acad. Sci. U.S.A. 108:9619-9624(2011) Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody.McLellan J.S., Chen M., Leung S., Graepel K.W., Du X., Yang Y., Zhou T., Baxa U., Yasuda E., Beaumont T., Kumar A., Modjarrad K., Zheng Z., Zhao M., Xia N., Kwong P.D., Graham B.S.Science 340:1113-1117(2013) Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus.McLellan J.S., Chen M., Joyce M.G., Sastry M., Stewart-Jones G.B., Yang Y., Zhang B., Chen L., Srivatsan S., Zheng A., Zhou T., Graepel K.W., Kumar A., Moin S., Boyington J.C., Chuang G.Y., Soto C., Baxa U., Bakker A.Q., Spits H., Beaumont T., Zheng Z., Xia N., Ko S.Y., Todd J.P., Rao S., Graham B.S., Kwong P.D.Science 342:592-598(2013)

NCBI and Uniprot Product Information

NCBI GI #
UniProt Accession #
Molecular Weight
57.9 kDa
NCBI Official Full Name
Fusion glycoprotein F0
UniProt Protein Name
Fusion glycoprotein F0
UniProt Gene Name
F
UniProt Synonym Gene Names
Protein F
UniProt Entry Name
FUS_HRSVA

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Product Notes

The F f (Catalog #AAA18595) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 27-529aa; Full Length of Mature Protein. The amino acid sequence is listed below: NITEEFYQST CSAVSKGYLS ALRTGWYTSV ITIELSNIKE NKCNGTDAKV KLIKQELDKY KNAVTELQLL MQSTPPTNNR ARRELPRFMN YTLNNAKKTN VTLSKKRKRR FLGFLLGVGS AIASGVAVSK VLHLEGEVNK IKSALLSTNK AVVSLSNGVS VLTSKVLDLK NYIDKQLLPI VNKQSCSISN IETVIEFQQK NNRLLEITRE FSVNAGVTTP VSTYMLTNSE LLSLINDMPI TNDQKKLMSN NVQIVRQQSY SIMSIIKEEV LAYVVQLPLY GVIDTPCWKL HTSPLCTTNT KEGSNICLTR TDRGWYCDNA GSVSFFPQAE TCKVQSNRVF CDTMNSLTLP SEINLCNVDI FNPKYDCKIM TSKTDVSSSV ITSLGAIVSC YGKTKCTASN KNRGIIKTFS NGCDYVSNKG MDTVSVGNTL YYVNKQEGKS LYVKGEPIIN FYDPLVFPSD EFDASISQVN EKINQSLAFI RKSDELLHNV NAGKSTTNIM ITT. It is sometimes possible for the material contained within the vial of "Fusion glycoprotein F0 (F), Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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