SARS-COV-2 (COVID-19, 2019-nCoV) Reagents
SARS-CoV-2 (COVID-19) | SARS-CoV | SARS-CoV-2 (COVID-19) Background
SARS-CoV-2 (COVID-19) Virus Antibody Research
ProSci has developed and manufactured SARS-CoV-2 (COVID-19) antibodies, antigens, and other reagents related to cellular entry: ACE2 receptor, TMPRSSR2 protease, and furin enzyme. ProSci is continuously adding new SARS-CoV-2 (COVID-19) reagents for spike, S1, S2, nucleocapsid, membrane, envelope including llama single domain antibodies and recombinant proteins.
| SARS-CoV-2 Featured Products | ||
|---|---|---|
|
COVID-19 Patient Validated Cat. No: 9083 SARS-CoV-2 (COVID-19) Spike S1 Antibody
|
COVID-19 Patient Validated Cat. No: 3525 SARS-CoV-2 (COVID-19) Spike Antibody
|
COVID-19 Patient Validated Cat. No: 3531 SARS-CoV-2 (COVID-19) Envelope Antibody
|
SARS-CoV-2 (COVID-19) Antibody Reagents
ProSci offers a comprehensive list of SARS-CoV-2 (COVID-19) antibodies against viral proteins; spike, nucleocapsid, envelope, ORF, and NSP. These antibodies can be used with various applications: IHC, Flow Cytometry, ELISA, WB, and Lateral-Flow.
SARS-CoV-2 (COVID-19) Recombinant Protein
Recombinant proteins expressed in various cell lines and expression systems for the novel coronavirus SARS-CoV-2 (COVID-19): Full/partial length, tagged/untagged, and biologically active.
SARS-CoV Reagents
In addition to our coronavirus COVID-19 (SARS-CoV-2) antibodies & recombinant proteins, similar related reagents are available for SARS-CoV. The two viruses, SARS-CoV-2 and SARS-CoV, have approximately 79% sequence identity. For potential antibody cross reactivity refer to the table below.
SARS-CoV Antibodies
| Product | Cat. No. | Host | Application | Clonality | Protein Structure | Identity | Homology | Blocking Peptide |
|---|---|---|---|---|---|---|---|---|
| SARS Spike Antibody | 3221 | Rabbit | ELISA | Polyclonal | Spike Protein | 56% | 69% | Blocking Peptide |
| SARS Spike Antibody | 3225 | Rabbit | ELISA | Polyclonal | Spike Protein | 38% | 56% | Blocking Peptide |
| SARS Spike Antibody | 3219 | Rabbit | ELISA | Polyclonal | Spike Protein | 14% | 29% | Blocking Peptide |
| SARS Matrix Antibody | 3527 | Rabbit | ELISA | Polyclonal | Membrane Protein | 86% | 93% | Blocking Peptide |
| SARS Matrix Antibody | 3529 | Rabbit | ELISA | Polyclonal | Membrane Protein | 80% | 93% | Blocking Peptide |
| SARS Envelope Antibody | 3533 | Rabbit | ELISA | Polyclonal | Envelope Protein | 82% | 91% | Blocking Peptide |
SARS-CoV Recombinant Protein
| Product | Cat. No. | Source | Fusion Tag | Sequence |
|---|---|---|---|---|
| SARS S Recombinant Protein | 97-094 | HEK293 | His Tag | Ser 14 - Pro 1195 |
For COVID-19(SARS-CoV-2) receptor reagents, check out our ACE2 products! In addition to all our COVID-19 related antibody reagents, we also offer custom antibody services for polyclonal, monoclonal, and single domain antibodies.
SARS-CoV-2 (COVID-19) Background
COVID-19 is an acute respiratory disease caused by novel coronavirus SARS-CoV-2 also known as 2019-nCoV. On March 11, 2020, the World Health Organization (WHO) characterized COVID-19 as a pandemic[i]. COVID-19 coronavirus SARS-CoV-2 belongs to the Betacoronavirus genus originating from bats. Betacoronaviruses can infect mammals, are zoonotic pathogens, and can cause severe respiratory disease in humans. Other viruses in this family are SARS coronavirus and MERS coronavirus. COVID-19 (SARS-CoV-2) has approximately 79% sequence identity to SARS-CoV and 50% to MERS-CoV.[ii] In addition, homology modeling shows COVID-19 (SARS-CoV-2) has a similar receptor-binding domain structure as SARS-CoV which suggests SARS-CoV-2 uses ACE2 receptor in humans for infection.
SARS-CoV-2 (COVID-19) Structure
The structure[iii] of COVID-19 (SARS-CoV-2) consists of the following: a spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA as seen in the figure below.
|
|
Spike protein (S) is heavily glycosylated, utilizes an N-terminal signal sequence to gain access to the ER and mediate attachment to host receptors. It is the largest structure and makes the distinct spikes on the surface of the virus. For SARS-CoV-2, S protein is cleaved by cellular furin-like protease TMPRSS2[iv] into two separate polypeptides S1 and S2. S1 also consists of a receptor binding domain(RBD) which binds to virus receptor ACE2 RNA is the genome of the virus.
Nucleocapsid protein (N) binds to RNA in vitro and is heavily phosphorylated. N proteins binds the viral genome in a beads on a string type conformation. This protein likely helps tether the viral genome to replicase-transcriptase complex (RTC), and subsequently package the encapsulated genome into viral particles. Envelope protein (E) is found in small quantities in within the virus. It is most likely a transmembrane protein and with ion channel activity. The protein facilitates assembly and release of the virus and has other functions such as ion channel activity. It is not necessary for viral replication but it is for pathogenesis. Membrane protein (M) is the most abundant structural protein. It does not contain signal sequence and exists as a dimer in the virion. It may have two different conformations to enable it to promote membrane curvature as well as bind to nucleocapsid. Hemagglutinin-esterase dimer protein (HE) is present in a subset of betacoronaviruses. The protein binds sialic acids on surface glycoproteins. The protein activities are thought to enhance S protein-mediated cell entry and virus spread through the mucosa. |
[i] World Health Organization "WHO Director-General's opening remarks at the media briefing on COVID-19 - 11 March 2020" https://www.who.int/dg/speeches/detail/who-director-general-s-opening-remarks-at-the-media-briefing-on-covid-19---11-march-2020
[ii] Lu R, Zhao X, Li J, et al. Genomic characterization and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. The Lancet. Published online January 29, 2020. https://doi.org/10.1016/ S0140-6736(20)30251-8
[iii] Fehr AR, Perlman S. Coronaviruses: an overview of their replication and pathogenesis. Methods Mol Biol. 2015;1282:1–23. https://doi.org/10.1007/978-1-4939-2438-7_1
[iv] Hoffmann, M., Kleine-Weber, H., Schroeder, S., et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. S0092–8674(20)30229–4 Advance online publication. https://doi.org/10.1016/j.cell.2020.02.052
