Recombinant Sendai virus Fusion glycoprotein F0 (F), partial

SKU: P04855

Size: 100ug. Other sizes are also available.

Activity: Not tested

Research Areas: Others

Uniprot ID: P04855

Gene Names: F

Alternative Name(s): (Protein F)

Abbreviation: Recombinant Sendai virus Fusion glycoprotein F0, partial

Organism: Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ))

Source: E.coli

Expression Region: 26-116aa

Protein Length: Partial

Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein Sequence: QIPRDRLSNIGVIVDEGKSLKIAGSHESRYIVLSLVPGVDFENGCGTAQVIQYKSLLNRLLIPLRDALDLQEALITVTNDTTQNAGAPQSR

MW: 17.3 kDa

Purity: Greater than 85% as determined by SDS-PAGE.

Endotoxin: Not test

Biological_Activity:

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℃/-80℃. 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℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ 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) interacts with HN tetramer 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: "Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein." Segawa H., Yamashita T., Kawakita M., Taira H. J. Biochem. 128: 65-72(2000)

Function: