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Bovine Coronavirus Spike Protein (AA 326-540, partial) (His tag)

BCoV S Origine: Bovine Coronavirus (BCoV) Hôte: Escherichia coli (E. coli) Recombinant > 90 % SDS
N° du produit ABIN5710878
  • Antigène Tous les produits Bovine Coronavirus Spike (BCoV S)
    Bovine Coronavirus Spike (BCoV S) (Bovine Coronavirus Spike Protein (BCoV S))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 326-540, partial
    Origine
    Bovine Coronavirus (BCoV)
    Source
    • 1
    Escherichia coli (E. coli)
    Purification/Conjugué
    Cette Bovine Coronavirus Spike protéine est marqué à la His tag.
    Application
    SDS-PAGE (SDS)
    Séquence
    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
    Pureté
    > 90 %
  • Indications d'application
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    0.1-2 mg/mL
    Buffer
    20 mM Tris-HCl based buffer, pH 8.0
    Stock
    -80 °C,4 °C,-20 °C
    Stockage commentaire
    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.
  • Antigène
    Bovine Coronavirus Spike (BCoV S) (Bovine Coronavirus Spike Protein (BCoV S))
    Autre désignation
    Bovine Corona Virus Peplomer Protein (BCoV S Produits)
    Classe de substances
    Viral Protein
    Sujet
    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 .
    Poids moléculaire
    27.7 kDa
    UniProt
    P25194
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