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SARS-CoV-2 Spike Protein (Trimer) (rho-1D4 tag)

Origine: SARS Coronavirus-2 (SARS-CoV-2) Hôte: HEK-293 Cells Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, SDS, WB, Crys
N° du produit ABIN6952670
  • Antigène Voir toutes SARS-CoV-2 Spike Protéines
    SARS-CoV-2 Spike
    Type de proteíne
    Recombinant
    Attributs du protein
    Trimer
    Origine
    • 223
    • 37
    • 9
    • 8
    • 7
    • 6
    • 6
    • 5
    • 4
    • 4
    • 3
    • 2
    • 1
    • 1
    SARS Coronavirus-2 (SARS-CoV-2)
    Source
    • 198
    • 7
    • 7
    • 3
    • 3
    • 3
    • 2
    • 1
    • 1
    • 1
    • 1
    HEK-293 Cells
    Purification/Conjugué
    Cette SARS-CoV-2 Spike protéine est marqué à la rho-1D4 tag.
    Application
    ELISA, SDS-PAGE (SDS), Western Blotting (WB), Crystallization (Crys)
    Fonction
    Trimeric, full length Cov-2 spike protein for assay development (""Antibody tests"")
    Specificité
    • single span transmembrane membrane protein (aa 1-1273)
    • Furin cleavage site ""RRAR"" mutated to ""GSAS""
    • trimerization (3 x 142 kDa) shown on native PAGE
    • expressed in Expi293™ cells
    • C-terminal Rho1D4 tag for affinity purification
    • Solubilization and stabilization in LMNG detergent
    • 2-step purification via Rho1D4 tag and size exclusion chromatography in LMNG detergent
    Attributs du produit
    • Made in Germany - from design to production - by highly experienced protein experts.
    • Full length SARS Cov-2 spike protein expressed in Expi293™ cells to assure native state glycosylation.
    • Purification by a multi-step, protein-specific protocol to ensure crystallization grade.
    • State-of-the-art algorithm used for plasmid design (Gene synthesis).

    The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.

    The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

    Purification
    The protein is purified from the cleared cell lysate using Rho1D4 capture materials. Eluate fractions are analyzed by SDS-PAGE.
    Protein containing fractions are subjected to a second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
    Pureté
    >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    niveau d'endotoxine
    Protein is endotoxin-free.
    Top Product
    Discover our top product SARS-CoV-2 Spike Protéine
  • Indications d'application
    In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a gurantee though.
    Commentaires

    Further modifications:
    - furin cleavage site "682-RRAR|SV-687" mutated to "682-GSAG|PP-687"
    - C-terminal Rho1D4 tag fused with spacer "GSSG" to protein sequence
    Size: 1286 amino acids (including Rho1D4 tag and linker)

    Restrictions
    For Research Use only
  • Buffer
    20 mM Hepes pH 7.5; 150 mM NaCl, 0.001 % LMNG
    Conseil sur la manipulation
    Avoid repeated freeze-thaw cycles.
    Stock
    -80 °C
    Date de péremption
    Unlimited (if stored properly)
  • Antigène
    SARS-CoV-2 Spike
    Abstract
    SARS-CoV-2 Spike Produits
    Synonymes
    E2 Protein, E2 glycoprotein precursor Protein, Surface Glycoprotein Protein, S Protein
    Classe de substances
    Viral Protein
    Sujet
    The spike glycoprotein exists as a homotrimeric fusion protein. Each of the trimers contains 66 glycosylation sites for host-derived N-linked glycans. Accordingly, expression of this primary target for SARS-CoV-2 vaccine development in an appropriate, human expression system is of utmost importance. Prior to ACE2 binding, each monomer in the prefusion complex contains an S1 ectodomain including the receptor binding domain (RBD) and an S2 endodomain harboring a transmembrane domain. In the predominant state of the trimer, one of the RBDs is in an “up” position whereas the other two are in a “down” position. Interaction of S-protein and ACE2 only takes place with the RBD in the “up” position. Receptor binding triggers a structural change that leads to separation of the S1 and S2 subunits.
    Poids moléculaire
    3 x 142 kDa
    ID gène
    43740568
    UniProt
    P0DTC2
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