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

Scan QR to view Datasheet Catalog #    MBS1072444
SDS-PAGE
Unit / Price
0.01 mg (E-Coli)  /  $150 +1 FREE 8GB USB
0.01 mg (Yeast)  /  $170 +1 FREE 8GB USB
0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
0.05 mg (Yeast)  /  $220 +1 FREE 8GB USB
0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
0.1 mg (Yeast)  /  $345 +1 FREE 8GB USB
0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
0.2 mg (Yeast)  /  $545 +1 FREE 8GB USB
0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
0.5 mg (Yeast)  /  $900 +1 FREE 8GB USB
0.05 mg (Baculovirus)  /  $1,130 +1 FREE 8GB USB
1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
0.05 mg (Mammalian-Cell)  /  $1,380 +1 FREE 8GB USB
1 mg (Yeast)  /  $1,410 +1 FREE 8GB USB
0.1 mg (Baculovirus)  /  $1,435 +1 FREE 8GB USB
0.5 mg (Baculovirus)  /  $2,055 +2 FREE 8GB USB
0.1 mg (Mammalian-Cell)  /  $2,080 +2 FREE 8GB USB
1 mg (Baculovirus)  /  $2,700 +3 FREE 8GB USB
 
 Go to:   rightarrow  Product Names   rightarrow Product Info   rightarrow Accession #s   rightarrow Product Desc   rightarrow Diseases/Tissues/Pathways   rightarrow Applications   rightarrow References 
 Product Name   

Fusion glycoprotein F0 (F), Recombinant Protein

★Popular Item★
 Also Known As   

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

 Product Gene Name   

F recombinant protein

[Similar Products]
 Research Use Only    For Research Use Only. Not for use in diagnostic procedures.
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 MBS1072444 COA    COA PDF
 Sequence Positions    27-529. Fragment at the N-terminal, provide the complete extracellular domain.
 Sequence    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 L AYVVQLP LYGVIDTPCW KLHTSPLCTT NTKEGSNICL TRTDRGWYCD NAGSVSFFPQ AETCKVQSNR VFCDTMNSLT LPSEINLCNV DIFNPKYDCK IMTSKTDVSS SVITSLGAIV SCYGKTKCTA SNKNRGIIKT FSNGCDYVSN KGMDTVSVGN TLYYVNKQEG KSLYVKGEPI INFYDPLVFP SDEFDASISQ VNEKINQSLA FIRKSDELLH NVNAGKSTTN IMITT
 3D Structure    ModBase 3D Structure for P03420
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 Host    E Coli or Yeast or Baculovirus or Mammalian Cell
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 Purity/Purification    Greater than 90% as determined by SDS-PAGE. (lot specific)
 Form/Format    Liquid containing glycerol
 Tag Information    This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
 Sterility    Sterile filter available upon request.
 Endotoxin    Low endotoxin available upon request.
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 Preparation and Storage    Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
 ISO Certification    Manufactured in an ISO 9001:2008 Certified Laboratory.
 Other Notes    Small volumes of F recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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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.
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 SDS-PAGE of F recombinant protein    F recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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NCBI/Uniprot data below describe general gene information for F. It may not necessarily be applicable to this product.
 NCBI GI #    138251
 NCBI Accession #    P03420.1 [Other Products]
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 UniProt Primary Accession #    P03420 [Other Products]
 UniProt Secondary Accession #    P88811 [Other Products]
 Molecular Weight    57.91kD
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 NCBI Official Full Name    Fusion glycoprotein F0
 UniProt Protein Name    Fusion glycoprotein F0
 UniProt Gene Name    F [Similar Products]
 UniProt Synonym Gene Names    Protein F [Similar Products]
 UniProt Entry Name    FUS_HRSVA
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 UniProt Comments for F    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 (PubMed:18216092). Interacts directly with heparan sulfate and may participates in virus attachment (PubMed:10864656). Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity (PubMed:11493675). 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 (PubMed:12663767).
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Product References and Citations for F recombinant protein

   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)
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 Precautions    All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
 Disclaimer    While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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