Fusion glycoprotein F0 (F), recombinant human metapneumovirus

Organism: Human metapneumovirus (strain CAN97-83) (HMPV). Source: in vitro E.coli expression system. Expression Region: 19-539aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 6xHis-SUMO-tagged. Target Protein Sequence: LKESYLEESC STITEGYLSV LRTGWYTNVF TLEVGDVENL TCSDGPSLIK TELDLTKSAL RELKTVSADQ LAREEQIENP RQSRFVLGAI ALGVATAAAV TAGVAIAKTI RLESEVTAIK NALKTTNEAV STLGNGVRVL ATAVRELKDF VSKNLTRAIN KNKCDIDDLK MAVSFSQFNR RFLNVVRQFS DNAGITPAIS LDLMTDAELA RAVSNMPTSA GQIKLMLENR AMVRRKGFGI LIGVYGSSVI YMVQLPIFGV IDTPCWIVKA APSCSGKKGN YACLLREDQG WYCQNAGSTV YYPNEKDCET RGDHVFCDTA AGINVAEQSK ECNINISTTN YPCKVSTGRH PISMVALSPL GALVACYKGV SCSIGSNRVG IIKQLNKGCS YITNQDADTV TIDNTVYQLS KVEGEQHVIK GRPVSSSFDP IKFPEDQFNV ALDQVFENIE NSQALVDQSN RILSSAEKGN TGFIIVIILI AVLGSSMILV SIFIIIKKTK KPTGAPPELS GVTNNGFIPH S. Purity: Greater than 85% 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: [Fusion glycoprotein F0]: Inactive precursor that is cleaved to give rise to the mature F1 and F2 fusion glycoproteins. [Fusion glycoprotein F1]: 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. [Fusion glycoprotein F2]: 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 . Reference: "Human metapneumovirus (HMPV) binding and infection are mediated by interactions between the HMPV fusion protein and heparan sulfate." Chang A., Masante C., Buchholz U.J., Dutch R.E. J. Virol. 86:3230-3243(2012). Function: nan