
Thermo Fisher Scientific Measles Virus Fusion Protein Polyclonal Antibody
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Applications
Tested Dilution
Publications
Immunohistochemistry (Paraffin) (IHC (P))
1:500-1,000
Immunohistochemistry (Frozen) (IHC (F))
1:50-200
Immunocytochemistry (ICC/IF)
1:50-200
ELISA (ELISA)
1:500-1:1,000
Product Specifications
Species Reactivity
Virus
Host/Isotype
Rabbit / IgG
Class
Polyclonal
Type
Antibody
Immunogen
KLH conjugated synthetic peptide derived from Measles virus fusion protein.
Conjugate
Unconjugated Unconjugated Unconjugated
Form
Liquid
Concentration
1 mg/mL
Purification
Protein A
Storage buffer
0.01M TBS, pH 7.4, with 1% BSA, 50% glycerol
Contains
0.02% ProClin 300
Storage conditions
-20°C
Shipping conditions
Ambient (domestic); Wet ice (international)
Target Information
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 H 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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