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SARS-CoV-2 is a virulent coronavirus, similar in structure to the SARS-CoV virus that was responsible for the 2002 SARS pandemic, that causes the infectious disease COVID-19. Through our brands, we offer an unparalleled selection of research tools for the study of SARS-CoV-2 and COVID-19.

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Antibody for Custom Assay Solutions

Antibodies for Coronavirus Research

Bio-Techne offers a large selection of antibodies for SARS‑CoV‑2 and COVID‑19 research. Our antibodies are essential tools that have supported pivotal research on SARS‑CoV‑2 recognition and viral infection and are being used to develop assays for SARS‑CoV‑2 detection.

coronavirus variants

R&D Systems™ Proteins for Coronavirus Research

R&D Systems, a Bio-Techne brand, offers a wide selection of recombinant proteins for SARS‑CoV‑2 research, including the U.K. and South African variant Spike proteins. All of our proteins are produced and purified in-house and are rigorously tested for bioactivity and lot-to-lot consistency.

Mechanism of SARS-CoV-2 viral cell entry

Tocris™ Small Molecules for COVID‑19 Research

Bio‑Techne, through the Tocris brand, provides a wide range of small molecules for exploring different stages of the SARS‑CoV‑2 viral lifecycle. The Tocris catalog offers products for targets involved in viral cell entry, including ACE2, TMPRSS2, and targets important in viral replication, such as Mpro, PLpro and RNA polymerase. The range includes FDA approved drugs, innovative new compounds, as well as fluorescent reagents.

LlaMABody™-Camelid Antibodies for Coronavirus Research

Our SARS-CoV-1/2 Spike RBD LlaMABody Recombinant Antibody is produced using the VHH72 CoV-2 RBD Blocking/Neutralization clone that was published by Wrapp, D. et al. in Cell. Learn more about this camelid antibody and our LlaMABody product line on the R&D Systems website, a Bio-Techne brand. 

Background Information

What is SARS-CoV-2?

SARS-CoV-2 is a virulent coronavirus, similar in structure to the SARS-CoV virus that was responsible for the 2002 SARS pandemic, that causes the infectious disease COVID-19. SARS-CoV-2 is a ~30-kb positive single-stranded RNA virus and has a genome organization that is similar to that of SARS-CoV, with both being organized into two main open reading frames (ORFs) and several smaller downstream ORFs. Two large ORFs, ORF1a and ORF1b, encode two polyproteins which are cleaved by viral encoded proteases resulting in several non-structural proteins (nsp). ORF1a encodes a 440-500 kDa polypeptide (pp1a) which is enzymatically processed to generate 11 nsps. The second ORF, ORF1b, encodes a larger polypeptide (pp1ab) of 740-810 kDa which is cleaved to generate 16 nsps.

SARS-CoV-2 genome organization

What Are SARS-CoV-2 Structural Proteins? 

Four major structural proteins have been identified in SARS-CoV-2 including spikenucleocapsidmembrane, and envelope proteins, which share significant identity with SARS-CoV. These four structural proteins are encoded by ORF2-10 and are required for viral coat formation and genome encapsidation. Compared to nsps, structural proteins elicit higher immune responses, both humoral and cellular mediated. While the main structural proteins have been well characterized, the ORF accessory proteins and nsps are in general less understood.

SARS-CoV-2 Spike Protein​

The spike protein in SARS-CoV-2 (1,273 aa) is a viral surface glycoprotein with two major functional domains, the S1 (14-667 aa) and S2 (668-1255 aa) domains, which mediate cell receptor binding and membrane fusion, respectively. Viral attachment and entry into host cells is dependent on the interaction of the spike’s receptor-binding domain (RBD: 306-527 aa) with specific cellular proteins. The angiotensin converting enzyme 2 (ACE-2) and the protease TMPRSS2 have been identified as the cellular receptor and priming protease required for SARS-CoV-2 cellular entry, respectively. The protease TMPRSS2 and/or cathepsin L cleave the spike protein at the S1-S2 junction, allowing the fusion of viral envelope and cellular membranes required for viral entry. SARS-CoV-2 may also be cleaved by furin which recognizes a four amino acid sequence at the S1-S2 junction. Besides cleavage of the spike protein at the S1-S2 junction, cellular proteases cleave the S2 subunit at a recognized S2’ sequence which is critical for activation of the spike protein and consequent membrane fusion.​ The surface glycoprotein or spike protein of SARS-CoV-2 shares 76% sequence identity with SARS-CoV's spike protein. 

SARS-CoV-2 Nucleocapsid Protein 

The nucleocapsid phosphoprotein (419 aa) is located within the core of the SARS-CoV-2 viral particle and interacts with the viral RNA. During viral assembly, the nucleocapsid protein plays a central role in packing the viral RNA genome. This process is dependent on its ability to self-associate as previously determined for the SARS-CoV nucleocapsid protein. SARS-CoV nucleocapsid protein has been implicated in other functions such as the modulation of host cellular processes including cell cycle deregulation, inhibition of IFN production, and induction of proinflammatory factors (e.g., COX-2).​ SARS-CoV-2 nucleocapsid protein shares 91% sequence identity with the SARS-CoV protein.

SARS-CoV-2 Membrane and Envelope Proteins 

The membrane (222 aa) and envelope (75 aa) proteins are integral proteins that function in viral assembly. SARS-CoV’s membrane protein is known to elicit the production of neutralizing antibodies in SARS patients while the envelope protein plays a role in SARS-CoV virulence and functions as an ion channel.​ SARS-CoV-2 membrane protein shares 91% sequence identity and the SARS-CoV-2 envelope protein shares 95% sequence identity with the respective SARS-CoV proteins.