Recombinant SARS-CoV-2 Spike Protein, S1 Subunit, Host Cell Receptor Binding Domain (RBD)

Referência 230-01102-100

Tamanho : 100ug

Marca : RayBiotech

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Recombinant SARS-CoV-2 Spike Protein, S1 Subunit, Host Cell Receptor Binding Domain (RBD), Antigen Grade

Recombinant SARS-CoV-2 Spike Protein, S1 Subunit, Host Cell Receptor Binding Domain (RBD) derived from E.coli
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Product Description

Specifications

Size100 µg, 500 µg, 1000 µg
SpeciesSARS-CoV-2
Accession Number
QHD43416
Protein Name / Synonyms
SARS-CoV-2 Spike Protein, S1 Subunit, S protein, spike protein
Expressed Region
Arg319 - Phe541
Expression SystemE. coli
TagN-terminal histidine tag
Purity
>95 %
Purity Determined BySDS-PAGE under reducing conditions and visualized by Coomassie blue staining
Molecular Weight (kDa)
∼25 kDa
Format
Liquid
Formulation
Filtered solution in 50 mM Na2HPO4 (pH 7.4), 0.5 M NaCl, 450 mM imidazole, 6 M urea.
Concentration (lot specific)
Lot specific (see the label on the vial), determined by Bradford protein assay.
Research AreaInfectious Disease, COVID-19
Shipping TypeBlue ice
Storage-20°C

Introduction

SARS-CoV-2 enters human cells by engaging the ACE2 receptor through the receptor-binding domain (RBD) in its spike protein. This RBD, located within the S1 subunit, is responsible for the initial viral attachment and is a major target for neutralizing antibodies and vaccine strategies. Blocking this interaction is a key approach in antiviral drug development.

Reference: https://link.springer.com/chapter/10.1007/978-3-031-46545-1_13

SDS-PAGE Image
Storage/Stability
Upon arrival, the protein may be stored for 2 weeks at 4°C. For long term storage, it is recommended to store at -20°C or -80°C in appropriate aliquots. Avoid repeated freeze-thaw cycles.

Disclaimer

"Antigen Grade" is not a formally regulated industry standard, but it is commonly used to indicate that a protein is intended for antigen-based applications rather than functional assays.

Antigen Grade proteins are recombinant proteins purified under denaturing conditions (e.g., in urea) and may not retain their native conformation or biological activity. These proteins are suitable for antigen-based applications such as antibody generation, ELISA plate coating, Western blotting, and other immunological assays, but are not recommended for functional or activity assays.

Suitable Applications:
✔ Antibody production (immunogen)
✔ ELISA coating antigen
✔ Western blot positive control
✔ Dot blot
✔ Epitope mapping
✔ Antibody screening, etc.

Not Recommended:
✘ Enzyme activity assays
✘ Ligand-receptor binding assays (unless validated)
✘ Cell-based functional assays
✘ SPR/BLI kinetic studies requiring native folding

Why "Antigen Grade"?

Many bacterial proteins expressed as inclusion bodies are purified in 6–8 M urea. Although they can often be refolded, proteins sold in urea are generally not guaranteed to be correctly refolded or biologically active. "Antigen Grade" proteins are suitable for immunological applications but may not be appropriate for assays requiring native protein function.

citations

  • Physicochemical Nature of SARS-CoV-2 Spike Protein Binding to Human Vimentin

    Year:
    2023
    Journal Name:
    Acs Applied Materials & Interfaces
  • An ultra-sensitive electrochemical biosensor using the Spike protein for capturing antibodies against SARS-CoV-2 in point-of-care

    Year:
    2022
    Journal Name:
    Materials Today Bio
  • Simultaneous Detection of SARS-CoV-2 Nucleoprotein and Receptor Binding Domain by a Multi-Area Reflectance Spectroscopy Sensor

    Year:
    2023
    Journal Name:
    Biosensors-Basel
  • Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies

    Species:
    Mouse
    Sample Type:
    Other / Unspecified (immunogen for BALB, c mice hybridoma production)
    Year:
    2024
    Journal Name:
    iScience
    PubMed ID:
    38500835
  • Direct activation of the alternative complement pathway by SARS-CoV-2 spike protein is blocked by factor D inhibition.Blood

    Year:
    2020
    PubMed ID:
    32877502
  • SARS-CoV-2 Spike Protein (RBD) Subunit Adsorption at Abiotic Surfaces and Corona Formation at Polymer Particles

    Year:
    2022
    Journal Name:
    International Journal of Molecular Sciences
  • SARS-CoV-2 Spike Protein Mutation at Cysteine-488 Impairs Its Golgi Localization and Intracellular S1/S2 Processing

    Year:
    2022
    Journal Name:
    International Journal of Molecular Sciences
  • ACE2-IgG1 fusions with improved in vitro and in vivo activity against SARS-CoV-2

    Year:
    2022
    Journal Name:
    iScience
    PubMed ID:
    34957381
  • Effects of spike proteins on angiotensin converting enzyme 2 (ACE2)

    Year:
    2023
    Journal Name:
    Archives of Biochemistry and Biophysics
  • Thermal analysis of protein stability and ligand binding in complex media

    Year:
    2022
    Journal Name:
    Thermochimica Acta

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