respiratory syncytial virus B Fusion glycoprotein F0 (F), partial, human, recombinant

Organism: Human respiratory syncytial virus B (strain B1). Source: Yeast. Expression Region: 137-574aa. Protein Length: Partial. Tag Info: N-terminal 6xHis-tagged. Target Protein Sequence: FLGFLLGVGS AIASGIAVSK VLHLEGEVNK IKNALLSTNK AVVSLSNGVS VLTSKVLDLK NYINNQLLPI VNQQSCRISN IETVIEFQQK NSRLLEINRE FSVNAGVTTP LSTYMLTNSE LLSLINDMPI TNDQKKLMSS NVQIVRQQSY SIMSIIKEEV LAYVVQLPIY GVIDTPCWKL HTSPLCTTNI KEGSNICLTR TDRGWYCDNA GSVSFFPQAD TCKVQSNRVF CDTMNSLTLP SEVSLCNTDI FNSKYDCKIM TSKTDISSSV ITSLGAIVSC YGKTKCTASN KNRGIIKTFS NGCDYVSNKG VDTVSVGNTL YYVNKLEGKN LYVKGEPIIN YYDPLVFPSD EFDASISQVN EKINQSLAFI RRSDELLHNV NTGKSTTNIM ITTIIIVIIV VLLSLIAIGL LLYCKAKNTP VTLSKDQLSG INNIAFSK. Purity: Greater than 90% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. 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. Storage: 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. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: During virus entry, induces fusion of viral and cellular mbranes 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 mbrane 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. Reference: Respiratory syncytial virus (RSV)SH and G proteins are not essential for viral replication in vitro clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant.Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E., Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R., Sidhu M.S.Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997). Function: 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 participate 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.