SARS-CoV-2 Spike Antibody (CR3022) [Janelia Fluor® 669]

Novus Biologicals, part of Bio-Techne | Catalog # NBP2-90980JF669

Recombinant Monoclonal Antibody
Novus Biologicals, part of Bio-Techne

Key Product Details

Species Reactivity

SARS-CoV, SARS-CoV-2

Applications

ELISA, Immunocytochemistry/ Immunofluorescence, Neutralization, Surface Plasmon Resonance

Label

Janelia Fluor 669

Antibody Source

Recombinant Monoclonal Human IgG1 kappa Clone # CR3022

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

View all Spike Antibodies »

Product Specifications

Immunogen

The original monoclonal antibody was generated through an scFv library derived from a peripheral blood lymphocytes of a patient exposed to the SARS-CoV.

Specificity

This antibody binds to both SARS-CoV and SARS-CoV-2 with high affinity (PMID: 16796401 & 32065055). It binds the amino acids 318-510 in the S1 domain of the SARS-CoV Spike protein as well as SARS-CoV-2 (COVID-19) Spike protein. The antibody also binds to P462L-substituted S318-510 fragments of the SARS spike protein. The binding epitope is only accessible in the "open" confromation of the spike protein (Joyce et al. 2020).

Clonality

Monoclonal

Host

Human

Isotype

IgG1 kappa

Applications for SARS-CoV-2 Spike Antibody (CR3022) [Janelia Fluor® 669]

Application
Recommended Usage

ELISA

Optimal dilutions of this antibody should be experimentally determined.

Immunocytochemistry/ Immunofluorescence

Optimal dilutions of this antibody should be experimentally determined.

Surface Plasmon Resonance

Optimal dilutions of this antibody should be experimentally determined.

Neutralization

Optimal dilutions of this antibody should be experimentally determined.
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Purification

Protein A purified

Formulation

50mM Sodium Borate

Preservative

0.05% Sodium Azide

Concentration

Please see the vial label for concentration. If unlisted please contact technical services.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C in the dark.

Background: Spike

The SARS-CoV-2 Spike protein is one of the four major structural proteins of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 (1,2). The spike protein is the largest of the structural proteins, which also include the membrane (M), envelope (E), and nucleocapsid (N) proteins (1,2). The SARS-CoV-2 spike protein is a 1273 amino acid (aa) heterotrimeric class I fusion protein with each monomer having a theoretical molecular weight of approximately 180 kDa (1). The club-shaped spike protein contains several functional regions and domains including the S1 globular head region which contains the N-terminal receptor-binding domain (RBD) and the S2 stem region that contains the C-terminal fusion domain, two heptad regions, a transmembrane domain, and a cytoplasmic tail (1,2). The viral spike protein is critical for attachment of the virus with the host cell, resulting in fusion and virus entry into the cell (1,2). More specifically, the RBD of the spike protein is responsible for binding to the cell surface receptor angiotensin converting enzyme 2 (ACE2) (1,2). This spike-ACE2 interaction results in a conformational change permitting furin cleavage between the S1 and S2 domains and then cleavage at S2' by TMPRRS2, or another protease, allowing membrane fusion (1,2).

Given the critical role of the spike protein RBD in the interaction with the ACE2 receptor and viral entry, a number of neutralizing antibodies against the RBD have been developed as potential therapeutics for treating COVID-19 (3). These antibodies bind the RBD domain on the S1 subunit inhibiting the interaction with ACE2 (3). However, more studies need to be done as neutralizing antibodies can result in antibody-dependent enhancement, in which the viral entry and replication within the host cell is increased (4). One potential way to combat antibody-dependent enhancement is the use of nanobodies (4). Furthermore, there are currently several vaccine strategies that are in clinical trials, or recently federally approved, that utilize the spike protein in different forms (e.g. full length, S1 RBD, RBD-Fc, N-terminal) for protecting against SARS-CoV-2 infection (4,5). These vaccine strategies include DNA vaccines, viral vector-based vaccines, RNA vaccines, and subunit vaccines (4,5).

References

1. Pillay T. S. (2020). Gene of the month: the 2019-nCoV/SARS-CoV-2 novel coronavirus spike protein. Journal of Clinical Pathology. https://doi.org/10.1136/jclinpath-2020-206658

2. Malik Y. A. (2020). Properties of Coronavirus and SARS-CoV-2. The Malaysian Journal of Pathology.

3. Ho M. (2020). Perspectives on the development of neutralizing antibodies against SARS-CoV-2. Antibody Therapeutics. https://doi.org/10.1093/abt/tbaa009

4. Samrat, S. K., Tharappel, A. M., Li, Z., & Li, H. (2020). Prospect of SARS-CoV-2 spike protein: Potential role in vaccine and therapeutic development. Virus Research. https://doi.org/10.1016/j.virusres.2020.198141

5. Sternberg, A., & Naujokat, C. (2020). Structural features of coronavirus SARS-CoV-2 spike protein: Targets for vaccination. Life Sciences. https://doi.org/10.1016/j.lfs.2020.118056

Long Name

Spike Protein

Alternate Names

S Protein

Gene Symbol

S

Additional Spike Products

Product Documents for SARS-CoV-2 Spike Antibody (CR3022) [Janelia Fluor® 669]

Product Datasheets

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Download SDS

Product Specific Notices for SARS-CoV-2 Spike Antibody (CR3022) [Janelia Fluor® 669]



Sold under license from the Howard Hughes Medical Institute, Janelia Research Campus.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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