30% OFF COVID-19 PROTEINSSale on recombinant proteins expressed in E. coli or human HEK293 cells.Promo code 30SARS-2021US direct customers only; Cannot be combined with any other offer. Expires December 31, 2021.
The SARS-CoV-2 virus, which is responsible for COVID-19, is comprised of nearly 30 proteins, including the Spike and Nucleocapsid proteins (see figures below). RayBiotech offers a comprehensive catalog of recombinant SARS-CoV-2 proteins.
Figure 1. SARS-CoV-2 Spike (S) protein domains. The virus gains entry into host cells through the interaction between the Spike protein’s receptor binding domain (RBD) and the host’s ACE2 receptor (cat no. 230-30165, 230-30177). The numbers below the domains show the amino acid position.Figure 2. SARS-CoV-2 Nucleocapsid protein domains. RBD = RNA binding domain; IDR = intrinsically disordered region; SR = serine-arginine-rich; NLS = nuclear localization signal.
Other Coronavirus Proteins
Like SARS-CoV-2, other coronaviruses can cause respiratory tract infections, including SARS-CoV, the Middle East respiratory syndrome coronavirus (MERS-CoV), and the human coronavirus HKU1 (HCoV-HKU1).
Angiotensin I Converting Enzyme 2 (ACE2) is an endogenous receptor that is required for SARS-CoV-2 viral entry. Other host receptors, Neuropilin-1 (NRP1), Tyrosine Kinase Receptor UFO (AXL), Basignin (or CD147), and Heat Shock Protein Family A Member 5 (GRP-78) have also been demonstrated to assist in SARS-CoV-2 entry.
The inflammation associated with SARS-CoV-2 infection can cause disseminated intravascular coagulopathy (DIC), leading to obstruction of the blood vessels of lung, heart and kidneys. Initially, DIC in COVID-19 patients presents with abnormalities in prothrombin time, partial thromboplastin time, and platelet counts.
Antonopoulos A, et al. Site-specific characterisation of SARS-CoV-2 spike glyocprotein receptor binding domain. Glycobiology, cwaa085 (2020). [view publication] RayBiotech Protein:Spike RBD
Beltrán-Pavez C, et al. Insights into neutralizing antibody responses in individuals exposed to SARS-CoV-2 in Chile. Science Advances (2021). [view publication] RayBiotech Protein:Spike RBD
Borchers C, et al. Evaluation of SARS-CoV-2 spike S1 protein response on PI3K-mediated IL-8 release. Med Sci (Basel) 18;9(2):30 (2021). [view publication] RayBiotech Protein:Spike RBD
Bortolotti D, et al. SARS-CoV-2 spike 1 protein controls natural killer cell activation via the HLA-E/NKG2A pathway. Cells (2020). [view publication] RayBiotech Protein:Spike Subunit 1, Spike Subunit 2
Bray RA, et al. Development and validation of a multiplex, bead-based assay to detect antibodies directed against SARS-CoV-2 proteins. Buzhdygan TP, et al. The SARS-CoV-2 spike protein alters barrier function in 2D static and 3D microfluidic in-vitro models of the human blood-brain barrier. Neurobiol Dis. 146: 105131 (2020). [view publication] RayBiotech Protein: Spike Subunit 1 (cat no. 230–01101, 230–30161), Spike RBD, Spike Subunit 2
Casasanta M, et al. Microchip-based structure determination of low-molecular weight proteins using cryo-electron microscopy. Nanoscale (2021). [view publication] RayBiotech Protein:Nucleocapsid
Hudák A, et al. Contribution of Syndecans to the Cellular Entry of SARS-CoV-2. Int J Mol Sci (2021). [view publication] RayBiotech Protein:Spike Subunit 1
Keshavarz B, et al. Quantitative measurement of IgG to severe acute respiratory syndrome coronavirus-2 proteins using immunoCAP. Int Arch Allergy Immunol. 182(5):417-424 (2021). [view publication] RayBiotech Protein:Spike RBD, Nucleocapsid
Khan S, et al. SARS-CoV-2 spike protein induces inflammation via TLR2-dependent activation of the NF-kB pathway. bioRxiv: the preprint server for biology (2021). [view publication] RayBiotech Protein:Spike Subunit 1, Spike Subunit 2, Nucleocapsid
Miller CJ, et al. FN3-based monobodies selective for the receptor binding domain of the SARS-CoV-2 spike protein. N Biotechnol (2021). [view publication] RayBiotech Protein:Spike RBD
Nguyen-Contant P, et al. S Protein-Reactive IgG and Memory B Cell RayBiotech Proteinion after Human SARS-CoV-2 Infection Includes Broad Reactivity to the S2 Subunit. mBio. 11 (5) e01991-20 (2020). [view publication] RayBiotech Protein:Nucleocapsid
Norman M, et al. Ultrasensitive high-resolution profiling of early seroconversion in patients with COVID-19. Nat Biomed Eng (2020). [view publication] RayBiotech Protein:Nucleocapsid
Prompetchara E, et al. DNA vaccine candidate encoding SARS-CoV-2 spike proteins elicited potent humoral and Th1 cell-mediated immune responses in mice. PLOS ONE 16(3): e0248007 (2021). [view publication] RayBiotech Protein:Spike Subunit 1, Spike Subunit 2
Rhea EM, et al. The S1 protein of SARS-CoV-2 crosses the blood-brain barrier in mice. Nature Neuroscience, 24 (2021). [view publication] RayBiotech Protein:Spike Subunit 1
Vojdani A and Kharrazian D. Potential antigenic cross-reactivity between SARS-CoV-2 and human tissue with a possible link to an increase in autoimmune diseases. Clin Immunol. 217, 108480 (2020). [view publication] RayBiotech Protein:Spike Subunit 1, Nucleocapsid
Vojdani A, et al. Reaction of human monoclonal antibodies to SARS-CoV-2 proteins with tissue antigens: implications for autoimmune diseases. Front Immunol (2021). [view publication] RayBiotech Protein:Spike Subunit 1, Nucleocapsid
Woodruff M, et al. Extrafollicular B cell responses correlate with neutralizing antibodies and morbidity in COVID-19. Nature Immunology (2020). [view publication] RayBiotech Protein:Nucleocapsid
Yu J, et al. Direct activation of the alternative complement pathway by SARS-CoV-2 spike protein is blocked by factor D inhibition. Blood. 2020 Sep 2;blood.2020008248 (2020). [view publication] RayBiotech Protein:Spike RBD, Spike Subunit 2, Nucleocapsid
