Bovine Coronavirus Spike Protein (AA 326-540, partial) (His tag)
BCoV S
Origin: Bovine Coronavirus (BCoV)
Host: Escherichia coli (E. coli)
Recombinant
> 90 %
SDS
1 image
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- Target See all Bovine Coronavirus Spike (BCoV S) products
- Bovine Coronavirus Spike (BCoV S) (Bovine Coronavirus Spike Protein (BCoV S))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 326-540, partial
- Origin
- Bovine Coronavirus (BCoV)
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This Bovine Coronavirus Spike protein is labelled with His tag.
- Application
- SDS-PAGE (SDS)
- Sequence
- PNLPDCNIEA WLNDKSVPSP LNWERKTFSN CNFNMSSLMS FIQADSFTCN NIEAAKIYGM CFSSITIDKF AIPNGRKVDL QLGNLGYLQS FNYRIDTTAA SCQLYYNLPA ANVSVSRFNP STWNRRFGFT EQSVFKPQPV GVFTHHDVVY AQHCFKAPTN FCPCKLDGSL CVGNGPGIDA GYKNSGIGTC PAGTNYLTCH NAAQCDCLCT PDPIT
- Purification
- SDS-PAGE
- Purity
- > 90 %
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 0.1-2 mg/mL
- Buffer
- 20 mM Tris-HCl based buffer, pH 8.0
- Storage
- -80 °C,4 °C,-20 °C
- Storage Comment
- Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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- Target
- Bovine Coronavirus Spike (BCoV S) (Bovine Coronavirus Spike Protein (BCoV S))
- Alternative Name
- Bovine Corona Virus Peplomer Protein (BCoV S Products)
- Target Type
- Viral Protein
- 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 .
- Molecular Weight
- 27.7 kDa
- UniProt
- P25194
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