SARS-CoV-2 Antibodies

With the outbreak of COVID-19 in the Chinese city of Wuhan, infection prevention and control has become critical. To support SARS-CoV-2 research we put together a large collection of antibodies against different SARS-CoV-2 targets. Products for spike protein, membrane protein, envelope protein, nucleocapsid protein and non structural proteins are available. These antibodies can be used for detection of the virus in a variety of applications including IHC, ELISA, WB, IF staining. We also offer a set of neutralizing antibodies based on clone CR3022. Discover our SARS-CoV-2 antibody portfolio below.

SARS-CoV-2 S Mutation Proteins

We support your research with reliable SARS-CoV-2 mutation proteins. B.1.1.7 / P.1 / B.1.351 / S Protein wild type. 400+ labs in diagnostics, pharma, academia have used our SARS-CoV-2 research tools.

Explore our variety of mutation proteins

Featured SARS-CoV-2 Antibodies used in Current Research

SARS-CoV-2 Spike Antibodies (S1, S2)

The SARS-CoV-2 spike protein protrudes from the envelope of the virion and plays a pivotal role in the receptor host selectivity and cellular attachment. Strong scientific evidence showed that SARS and SARS-CoV-2 spike proteins interact with angiotensin-converting enzyme 2 (ACE2).⁽¹⁾

Below you will find a selection of our SARS-CoV-2 spike protein antibodies. Click on the links to see more details. See neutralizing S-protein antibodies based on clone CR3022

See a complete SARS-CoV-2 S Antibody List

SARS-CoV-2 Nucleocapsid Antibodies

The nucleocapsid (N) protein is an important antigen for coronavirus, which participate in RNA package and virus particle release. After infection, the N protein enters the host cell together with the viral RNA to facilitate its replication and process the virus particle assembly and release. SARS-CoV N protein contains two distinct RNA-binding domains (NTD and CTD) linked by a poorly structured linkage region containing a serine/arginine-rich (SR-rich) domain. ⁽²⁾

Below you will find a selection of our CoV SARS-CoV Nucleocapsid protein antibodies.

Rabbit Monoclonal SARS-CoV-2 N-Protein Antibodies

Rabbit monoclonals offer an improved immune response to small epitopes and a better response to mouse antigens. They give a better reaction to antigens than those from rodents such as mice. Because of their advantages rabbit monoclonal antibodies are becoming more preferred in research and clinical applications.

SARS-CoV-2 N-Protein Antibodies

See a complete SARS-CoV-2 N Antibody List

SARS-CoV-2 Envelope Protein Antibodies

The E protein is the smallest of the major structural proteins of SARS-CoV-2 and participates in viral assembly and budding. During the replication cycle, E is abundantly expressed inside the infected cell, but only a small portion is incorporated into the virion envelope. The majority of the protein is localised at the site of intracellular trafficking.⁽³⁾ We currently offer two E-protein antibodies SARS-CoV-2 E-protein antibody ABIN1031551 and SARS-CoV-2 E-protein antibody ABIN6952904 .

Below you will find the available SARS-CoV-2 Envelope protein antibodies. Click on the links to see more details.

SARS-CoV-2 Membrane Protein Antibodies

The coronavirus membrane (M) protein is the key player in virion assembly. One of its functions is to mediate the incorporation of the spikes into the viral envelope. When expressed alone, it accumulates in the Golgi complex in homomultimeric complexes. However, in combination with the E protein, virus-like particles (VLPs) similar to authentic virions in size and shape are assembled, demonstrating that the M and E proteins are the minimal requirements for envelope formation.⁽⁴⁾ We currently offer one SARS-CoV-2 M-protein antibody (rabbit polyclonal for ELISA, WB).

Below you will find a selection of our SARS-CoV membrane protein antibodies. Click on the links to see more details.

See a complete SARS-CoV M Antibody List

SARS-CoV-2 ORF Antibodies

Neutralizing SARS-CoV-2 Antibody [CR3022]

Presently, we are offering a variety of recombinant NAbs against SARS-CoV-2 S1, based on clone CR3022. Click the link below to see all available CR3022 antibodies.

starrecommended

SARS-CoV-2 Spike S1 antibody (RBD)

• Recombinant human neutralizing antibody against SARS-CoV-2.
• Frequently used as reference in S-protein ELISAs and neutralization assays.
• Binds a highly conserved epitope, not interefering with the S-protein's ACE2 RBD.

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starrecommended

SARS-CoV-2 Spike S1 antibody (RBD)

• The chimeric SARS-CoV S1 antibody (CR3022) 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.
• Epitope does not overlap with ACE2-Binding Site.
• 7 PubMed References available.

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See a complete list of our neutralizing antibodies

References

• Florindo, H.F., Kleiner, R., Vaskovich-Koubi, D. et al. Immune-mediated approaches against COVID-19. Nat. Nanotechnol. 15, 630–645 (2020). https://doi.org/10.1038/s41565-020-0732-3
• Kandimalla, R., John, A., Abburi, C. et al. Current Status of Multiple Drug Molecules, and Vaccines: An Update in SARS-CoV-2 Therapeutics. Mol Neurobiol 57, 4106–4116 (2020). https://doi.org/10.1007/s12035-020-02022-0
• Ortega J. T., Serrano M. L., Pujol F. H., Rangel H. R. Role of changes in SARS-CoV-2 spike protein in the interaction with the human ACE2 receptor: An in silico analysis. EXCLI J. 2020; 19: 410–417. PMID: 32210742.
• Thao, T. T. N. et al. Rapid reconstruction of SARS-CoV-2 using a synthetic genomics platform. Nature https://doi.org/10.1038/s41586-020-2294-9 (2020).
• Weihong Zeng, Guangfeng Liu, Huan Ma, Dan Zhao et al. Biochemical characterization of SARS-CoV-2 nucleocapsid protein. Biochem Biophys Res Commun. 2020 Jun 30; 527(3): 618–623. PMID: 32416961
• de Haan CA, Smeets M, Vernooij F, Vennema H, Rottier PJ. Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein. J Virol. 1999 Sep;73(9):7441-52. PMID: 10438834; PMCID: PMC104271.
• Roujian Lu, Xiang Zhao, Juan Li, Peihua Niu, Bo Yang, Honglong Wu et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. January 30, 2020.