Fusion glycoprotein F0 (F), partial, recombinant Newcastle disease virus

Organism: Newcastle disease virus (strain Her/33) (NDV). Source: E.coli. Expression Region: 32-500aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: LDGRPLAAAG IVVTGDKAVN IYTSSQTGSI IVKLLPNMPK DKEACAKAPL EAYNRTLTTL LTPLGDSIRR KQESVTTSGG RRQRRFIGAI IGSVALGVAT AAQITAASAL IQANQNAANI LRLKESIAAT NEAVHEVTDG LSQIAVAVGK MQQFVNDQFN NTAQELDCIK ITQQVGVELN LYLTELTTVF GPQITSPALT QLTIQALYNL AGGNMDYLLT KLGVGNNQLS SLIGSGLITG NPILYDSQTQ ILGIQVTLPS VGNLNNMRAT YLETLSVSTT KGFASALVPK VVTQVGSVIE ELDTSYCIGT DLDLYCTRIV TFPMSPGIYS CLSGNTSACM YSKTEGALTT PYMALKGSVI ANCKMTTCRC ADPPGIISQN YGEAVSLIDR HSCNVLSLDG ITLRLSGEFD ATYQKNISIL DSQVIVTGNL DISTELGNVN NSISNALNKL EESNSKLDKV NVRLTSTSA. 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: 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 heptad repeat HR 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 F protein probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. Reference: n/a. Function: nan