Recombinant Bovine coronavirus Spike glycoprotein (S), partial

Category: Proteins
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CSB-EP333052BJO
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Product Name Recombinant Bovine coronavirus Spike glycoprotein (S), partial
Description S1 attaches the virion to the cell mbrane by binding to 9-O-acetylated sialic acid containing proteins, initiating the infection.S2 is a 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 target cell mbrane fusion, the coiled coil regions (heptad repeats) 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 target cell mbranes .
Synonyms E2, Peplomer protein
Host E.coli
Molecular Weight 27.7
Amino Acid Sequence PNLPDCNIEAWLNDKSVPSPLNWERKTFSNCNFNMSSLMSFIQADSFTCNNIEAAKIYGMCFSSITIDKFAIPNGRKVDLQLGNLGYLQSFNYRIDTTAASCQLYYNLPAANVSVSRFNPSTWNRRFGFTEQSVFKPQPVGVFTHHDVVYAQHCFKAPTNFCPCKLDGSLCVGNGPGIDAGYKNSGIGTCPAGTNYLTCHNAAQCDCLCTPDPIT
Protein Length Partial, 326-540aa
Tag N-terminal 6xHis-tagged
Reactivity Bovine
Applications SDS-PAGE
Form Liquid, in Tris-based buffer, 50% glycerol
Purity Greater than 90% as determined by SDS-PAGE.
References Comparison of the nucleotide and deduced amino acid sequences of the S genes specified by virulent and avirulent strains of bovine coronaviruses.Zhang X., Kousoulas K.G., Storz J.Virology 183:397-404(1991)
Background S1 attaches the virion to the cell mbrane by binding to 9-O-acetylated sialic acid containing proteins, initiating the infection.S2 is a 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 target cell mbrane fusion, the coiled coil regions (heptad repeats) 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 target cell mbranes .
Supplier Cusabio

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