Recombinant Sars-Cov Ma15

Description: Serum, plasma

Description: SARS-CoV-2 - Mpro ELISA IgG

Description: SARS-CoV-2 - Spike ELISA IgG

Description: SARS-CoV-2 - RBD ELISA IgG

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, DPP4, CEACAM etc.. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Protein S (PROS1) is glycoprotein and expressed in many cell types supporting its reported involvement in multiple biological processes that include coagulation, apoptosis, cancer development and progression, and the innate immune response. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2, DPP4, CEACAM etc.. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. It's been reported that 2019-nCoV can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Membrane glycoprotein is involved in the formation and budding of the viral envelope, that is, in the assembly and release of the virus, inhibiting IFN attack.

Description: Coronavirus envelope (E) proteins are short (100 residues) polypeptides that contain at least one transmembrane (TM) domain and a cluster of 2-3 juxtamembrane cysteines. These proteins are involved in viral morphogenesis and tropism, and their absence leads in some cases to aberrant virions, or to viral attenuation. In common to other viroporins, coronavirus envelope proteins increase membrane permeability to ions, plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis. Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.

Description: It's been reported that SARS-CoV-2 can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus that belongs to the Coronaviridae family 1. The SARS-CoV-2 genome, which shares 79.6% identity with SARS-CoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 2. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 3. Each ~180 kDa monomer contains two functional subunits, S1 (~700 a.a) and S2 (~600 a.a), that mediate viral attachment and membrane fusion, respectively. S1 contains two major domains, the N-terminal (NTD) and C-terminal domains (CTD). The CTD contains the receptor-binding domain (RBD), which binds to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells 3-5. Although both SARS-CoV and SARS-CoV-2 bind the ACE2 receptor, the RBDs only share ~73% amino acid identity, and the SARS-CoV-2 RBD binds with a higher affinity compared to SARS-CoV 3, 6. The RBD is dynamic and undergoes hinge-like conformational changes, referred to as the “down” or “up” conformations, which hide or expose the receptor-binding motifs, respectively 7. Following receptor binding, S1 destabilizes, and TMPRSS2 cleaves S2, which undergoes a pre- to post-fusion conformation transition, allowing for membrane fusion 8, 9. _x000D__x000D__x000D_Polyclonal RBD-specific antibodies can block ACE2 binding 10, 11, and anti-RBD neutralizing antibodies are present in the sera of convalescent COVID19 patients 12, identifying the RBD as an attractive candidate for vaccines and therapeutics. In addition, the RBD is poorly conserved, making it a promising antigen for diagnostic tests 13 14. Serologic tests for the RBD are highly sensitive and specific for detecting SARS-CoV-2 antibodies in COVID19 patients 13 15. Furthermore, the levels of anti-RBD antibodies correlated with SARS-CoV-2 neutralizing antibodies, suggesting the RBD could be used to predict an individual's risk of disease 13._x000D_

Description: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), is an enveloped, single-stranded, positive-sense RNA virus that belongs to the Coronaviridae family 1. The SARS-CoV-2 genome, which shares 79.6% identity with SARS-CoV, encodes four essential structural proteins: the spike (S), envelope (E), membrane (M), and nucleocapsid protein (N) 2. The S protein is a transmembrane, homotrimeric, class I fusion glycoprotein that mediates viral attachment, fusion, and entry into host cells 3. Each ~180 kDa monomer contains two functional subunits, S1 (~700 a.a) and S2 (~600 a.a), that mediate viral attachment and membrane fusion, respectively. S1 contains two major domains, the N-terminal (NTD) and C-terminal domains (CTD). In both SARS-CoV and SARS-CoV-2, the CTD contains the receptor-binding domain (RBD), which binds to the angiotensin-converting enzyme 2 (ACE2) receptor on host cells3-5. The NTD of SARS-CoV-2 does not bind to ACE26, and the function of NTD in SARS-CoV-2 infection is not well understood. In other CoVs, the NTD may promote attachment by binding to sugar moieties7 and might play a role in the conformational change of S2 required for membrane fusion8. While most neutralizing antibodies target the RBD domain and block receptor binding, potent neutralizing antibodies targeting NTD were isolated from convalescent COVID19 patients9, identifying the NTD as an attractive candidate for vaccines and therapeutics. In addition, the NTD is a promising antigen for diagnostic tests, as there is only 53.5% homology between the NTD of SARS-CoV-2 and SARS-CoV10.

Description: The Severe Acute Respiratory Syndrome (SARS) Coronavirus (CoV) is an enveloped, positive-stranded RNA viruses that can cause a severe respiratory disease. Its genome consists of a ∼30 kb linear, non-segmented, capped, polycistronic, polyadenylated RNA molecule, the first two-third of which is directly translated into two large polyproteins. These two polypeptides are processed into 16 non-structural proteins (nsps), forming the replicase complex, which is active in the cytoplasm in close association with cellular membranes. Nsp1 was proved to be able to suppress host gene expression by promoting host mRNA degradation and was involved in cellular chemokine deregulation. This virus evades the host innate immune response in part through the expression of its non-structural protein (nsp) 1, which inhibits both host gene expression and virus- and interferon (IFN)-dependent signaling. Thus, nsp1 is a promising target for drugs, as inhibition of nsp1 would make SARS-CoV more susceptible to the host antiviral defenses.

Description: The viral nonstructural protein 1 (nsP1) is the only membrane-associated protein that anchors the replication complex to the cellular membranes. NSP1 inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.

Description: During the formation of the coronaviral replication/transcription complex, essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsp's. Upon infecting host cells, coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins (nsp) responsible for the replication and transcription of the viral genome. non-structural proteins 7 (NSP7) forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.

Description: NSP8, forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. To ultimately combat the emerging COVID-19 pandemic, it is desired to develop an effective and safe vaccine against this highly contagious disease caused by the SARS-CoV-2 coronavirus. By investigating the entire proteome of SARS-CoV-2, six proteins, including the S protein and five non-structural proteins (nsp3, 3CL-pro, and nsp8-10) were predicted to be adhesins, which are crucial to the viral adhering and host invasion. The S, nsp3, and nsp8 proteins were also predicted by Vaxign-ML to induce high protective antigenicity.

Description: The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses. Targeting PLpro with antiviral drugs may have an advantage in not only inhibiting viral replication but also inhibiting the dysregulation of signaling cascades in infected cells that may lead to cell death in surrounding, uninfected cells.