目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T77510 | SARS-CoV | ||
SARS-CoV-2-IN-46 是一种 SARS-CoV-2 抑制剂。 | |||
T77516 | Antiviral SARS-CoV | ||
SARS-CoV-2-IN-39是一种 SARS-CoV-2 抑制剂,EC50 为 1 μM。 SARS-CoV-2-IN-39 具有抗病毒活性,通过抑制 SKP2 蛋白并稳定 BECN1 来抑制 SARS-CoV-2。 | |||
T77652 | Antiviral SARS-CoV | ||
SARS-CoV-2 3CLpro-IN-20 是一种共价的 SARS-CoV-2 3CLpro 抑制剂(IC50s: 0.43 μM,)。SARS-CoV-2 3CLpro-IN-20 具有潜在的抗病毒活性。 | |||
T60538 | SARS-CoV | ||
SARS-CoV-2-IN-14 是一种有效的、可口服的 SARS-CoV-2 抑制剂(IC50 :0.39 μM),是一种氯硝柳胺类似物。SARS-CoV-2-IN-14在人血浆和肝 S9 酶测定中比氯硝柳胺稳定性更强。SARS-CoV-2-IN-14以口服的方式给药可以提高其生物利用度和半衰期。 | |||
TN3651 | Others | ||
Cichoriin 对SARS-CoV-2有明显活性,是治疗重症COVID-19的潜在候选物质。 | |||
T9458 | SARS-CoV | ||
PF-00835231 是一种 CoV-2 半胱氨酸 3C 样蛋白酶抑制剂,对 SARS CoV-2 和 SARS CoV-1 3CLpro 的 IC50 分别为 0.27 nM 和 4 nM。它用于抗 SARS-CoV-2/COVID-19 的研究。 | |||
T9614 | SARS-CoV | ||
MERS-CoV-IN-1 对冠状病毒的活性具有优异的抑制作用,可用作预防冠状病毒引起疾病的药物组合物。 | |||
T3S1447 | SARS-CoV Ferroptosis | ||
Arteannuin B 与青蒿素共同存在,有强效抗疟活性,具有抗 SARS-CoV-2 的活性,EC50为 10.28 μM。 | |||
T40660 | IL Receptor SARS-CoV | ||
Kansuinine B 抑制由 IL-6 诱导的 Stat3 活化。 Kansuinine B 具有抗病毒活性,可用于 COVID-19 研究。 | |||
T8419 | SARS-CoV | ||
XP-59 是一种 SARS-CoV Mpro 抑制剂,其 Ki 值为 0.1 nM。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPJ-01450 | SARS-CoV-2 Helicase Protein (His & MBP) | SARS-CoV-2 | E. coli | ||
The non—structural protein 13 (nsp13) of SARS—CoV 2 is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. A basic biochemical characterization of nsp13 demonstrated that it can unwind both doublestranded DNA and RNA in a 5’-3’ direction, and it can hydrolyze all deoxyribonucleotide and ribonucleotide triphosphates. Helicases are motor proteins that utilize the energy derived from nucleotide hydrolysisto unwind double-stranded nucleic acids into two single-stranded nucleic acids. Initially, helicases were only thought to be molecular engines that unwind nucleic acids during replication, recombination, and DNA repair. Recent studies have shown that they are also involved in other biological processes, including displacement of proteins from nucleic acid, movement of Holliday junctions, chromatin remodeling, catalysis of nucleic acid conformational changes, several aspects of RNA metabolism, including transcription, mRNA splicing, mRNA export, translation, RNA stability and mitochondrial gene expression. Some human diseases, including Bloom’s syndrome, Werner’s syndrome, and Xeroderma Pigmentosum have been associated with defects in helicase function.
|
|||||
TMPJ-01426 | SARS-CoV-2 NSP2 Protein (His) | SARS-CoV-2 | E. coli | ||
The positive-stranded RNA genome of the coronaviruses is translated from ORF1 to yield polyproteins that are proteolytically processed into intermediate and mature nonstructural proteins (nsps). SARS-CoV 2 polyproteins incorporate 16 protein domains (nsps). The putative non-structural protein 2 (nsp2) of SARS-CoV plays an important role in viral transcription and replication, and is an attractive target for anti-SARS drug development.
|
|||||
TMPJ-01425 | SARS-CoV-2 NSP1 Protein (His) | SARS-CoV-2 | E. coli | ||
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.
|
|||||
TMPJ-01427 | SARS-CoV-2 NSP7 Protein (His) | SARS-CoV-2 | E. coli | ||
The ∼30kb positive-stranded RNA genome of coronaviruses encodes a replication/transcription machinery that is unusually complex and composed of 16 nonstructural proteins (nsps). The four proteins nsp7 to nsp10, which are conserved among all CoVs but have no functional homologs outside of the Coronaviridae, are translated as part of the viral polyproteins pp1a and pp1ab, and the mature proteins are released by the action of the SARS-CoV protease nsp5. Hexadecamer of nsp7 and nsp8 may possess dsRNA-binding activity. SARS-CoV 2 nonstructural protein 7 (nsp7) is of interest for its potential roles in the transcription and replication of the positive-stranded viral RNA genome.
|
|||||
TMPJ-01428 | SARS-CoV-2 NSP8 Protein (His) | SARS-CoV-2 | E. coli | ||
Cleavage by the viral main protease, 3CLpro results in generating the nsp8 protein, The nsp8 protein has been shown to associate with several other nsps and to colocalize with these nsps in cytoplasmic complexes that are important for viral RNA synthesis. It 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.Nsp8 was shown to have RNA-dependent RNA polymerase (RdRp) activity that could be involved in producing primers utilized by nsp12 which is normally accepted to be the RdRp for SARS-CoV.
|
|||||
TMPY-02870 | SARS-CoV Nucleocapsid Protein (His) | SARS | Baculovirus-Insect Cells | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPJ-01429 | SARS-CoV-2 Guanine-N7 methyltransferase Protein (His) | SARS-CoV-2 | E. coli | ||
The nonstructural protein (nsp) 14 of SARS-CoV 2 was identified as a cap (guanine-N7)-methyltransferase (N7-MTase). Nsp14 of coronaviruses two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. It may be involved in the proof-reading ability during the viral RNA replication and transcription. GTP, dGTP as well as cap analogs GpppG, GpppA and m7GpppG could be methylated by nsp14.
|
|||||
TMPY-03224 | SARS-CoV Spike/RBD Protein (His) | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-04177 | SARS-CoV Spike/RBD Protein (rFc) | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05722 | SARS-CoV Spike S2 Protein (His) | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05701 | SARS-CoV Spike/RBD Protein (mFc) | SARS | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-03988 | SARS-CoV Spike/S1 Protein (His) | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05702 | SARS-CoV Spike/S1 Protein (mFc) | SARS | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05817 | SARS-CoV Spike/RBD Protein (His), Biotinylated | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06372 | SARS-CoV Spike RBD Protein (mFc), Biotinylated | SARS | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05699 | SARS-CoV Spike/S1 Protein (His), Biotinylated | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06204 | SARS-CoV (Isolate Tor2) Spike RBD Protein (His & Avi), Biotinylated | SARS | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06176 | SARS-CoV (Isolate Tor2) Spike S1+S2 Protein (S577A, His), Biotinylated | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05718 | SARS-CoV (Isolate Tor2) Spike S1+S2 ECD Protein (S577A, His) | SARS | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05679 | SARS-CoV-2 Spike RBD Protein (hFc) | SARS-CoV-2 | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPK-00265 | SARS-COV-2 Nucleocapsid Protein (His & Avi), Biotinylated | SARS-CoV-2 | E. coli | ||
Nucleocapsid protein (N) is the major viral structural component; its main function is to protect and encapsidate the viral RNA forming viral RNP complex. It is encoded by the S segment vRNA and is abundantly expressed in the cytoplasm of infected cells.
|
|||||
TMPY-06416 | SARS-CoV-2 NSP8 Protein | SARS-CoV-2 | E. coli | ||
NSP8 is a nonstructural protein of coronavirus. NSP8 acts as a primase in RNA synthesis. NSP8 and NSP7 are essential co-factors of NSP12 (the catalytic subunit with RNA-dependent RNA polymerase activity) that can remarkably stimulate RdRp activity. The nsp12-nsp7-nsp8 subcomplex is defined as the minimal core component for mediating coronavirus RNA synthesis.
|
|||||
TMPY-06012 | SARS-CoV-2 NSP10 Protein | SARS-CoV-2 | E. coli | ||
NSP10 is a major regulator of coronavirus replicase function. NSP10 contains two zinc fingers and binds and stimulates both NSP14 and NSP16 activities. Researchers has found that the nsp10 surface that interacts with nsp14 and nsp16 and possibly other subunits of the viral replication complex may be a target for the development of antiviral compounds against pathogenic coronaviruses.
|
|||||
TMPY-06009 | SARS-CoV-2 NSP7 Protein | SARS-CoV-2 | E. coli | ||
NSP7 is conserved within the coronaviridae. NSP7 is a component of the coronavirus replicase polyprotein to comprise a repilication complex. NSP7 has been shown to interact with NSP10 and NSP1 which indicate that NSP7 has a founction in coronavirus-specific RNA replication mechanisms.
|
|||||
TMPY-06011 | SARS-CoV-2 NSP10 Protein (His) | SARS-CoV-2 | E. coli | ||
NSP10 is a major regulator of coronavirus replicase function. NSP10 contains two zinc fingers and binds and stimulates both NSP14 and NSP16 activities. Researchers has found that the nsp10 surface that interacts with nsp14 and nsp16 and possibly other subunits of the viral replication complex may be a target for the development of antiviral compounds against pathogenic coronaviruses.
|
|||||
TMPY-05664 | SARS-CoV-2 Nucleocapsid Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-05749 | SARS-CoV-2 NSP8 Protein (Avi) | SARS-CoV-2 | E. coli | ||
NSP8 is a nonstructural protein of coronavirus. NSP8 acts as a primase in RNA synthesis. NSP8 and NSP7 are essential co-factors of NSP12 (the catalytic subunit with RNA-dependent RNA polymerase activity) that can remarkably stimulate RdRp activity. The nsp12-nsp7-nsp8 subcomplex is defined as the minimal core component for mediating coronavirus RNA synthesis.
|
|||||
TMPY-06086 | SARS-CoV-2 Helicase Protein (His) | SARS-CoV-2 | E. coli | ||
|
|||||
TMPY-05820 | SARS-CoV-2 NSP3 Protein (His) | SARS-CoV-2 | E. coli | ||
|
|||||
TMPY-04894 | SARS-CoV (strain WH20) Plpro/papain-like protease (His) | SARS | E. coli | ||
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.
|
|||||
TMPY-05681 | SARS-CoV-2 Spike RBD Protein (rFc) | SARS-CoV-2 | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06098 | SARS-CoV-2 Nucleocapsid Protein (I292T, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-06123 | SARS-CoV-2 Nucleocapsid Protein (P80R, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-06124 | SARS-CoV-2 Nucleocapsid Protein (T205I, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPJ-01431 | SARS-CoV-2 Papain-Like Protease Protein | SARS-CoV-2 | E. coli | ||
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.
|
|||||
TMPY-05663 | SARS-CoV-2 Spike RBD Protein (mFc) | SARS-CoV-2 | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05667 | SARS-CoV-2 Spike S1 Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06097 | SARS-CoV-2 Nucleocapsid Protein (S194L, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-06189 | SARS-CoV-2 Nucleocapsid Protein (A220V, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-06190 | SARS-CoV-2 Nucleocapsid Protein (P199L, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-05712 | SARS-CoV-2 NSP9 Protein (His & Avi) | SARS-CoV-2 | E. coli | ||
|
|||||
TMPY-06113 | SARS-CoV-2 Nucleocapsid CTD Protein (His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-05695 | SARS-CoV-2 Nucleocapsid Protein (His), Biotinylated | SARS-CoV-2 | Baculovirus-Insect Cells | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-06144 | SARS-CoV-2 Nucleocapsid Protein (D377Y, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-05693 | SARS-CoV-2 Methyltransferase/ME Protein (His) | SARS-CoV-2 | E. coli | ||
Coronavirus encodes the 2’-O-MTase (2'O Methyltransferase) that is composed of the catalytic subunit nsp16 and the stimulatory subunit nsp10 and plays an important role in virus genome replication and evasion from innate immunity during viral infection. Nonstructural protein 16 (NSP16) / viral 2'O-methyltransferase (2'O-MTase) is highly conserved. The conserved 2'O-MTase activity is important for CoV pathogenesis and NSP16 is a conserved universal target for rapid live attenuated vaccine design in an expanding Coronavirus outbreak setting, such as COVID-19. Targeting the 2'O-methylation pathway on SARS-CoV replication and pathogenesis can be the treatment options for vaccine and anti-viral drug development which can against SARS-CoV-2,SARS-CoV, MERS-CoV or other RNA and DNA viruses.
|
|||||
TMPY-05662 | SARS-CoV-2 Spike S1 Protein (mFc) | SARS-CoV-2 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
|
|||||
TMPY-06096 | SARS-CoV-2 Nucleocapsid Protein (P13L, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|
|||||
TMPY-05668 | SARS-CoV-2 Spike RBD Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-05660 | SARS-CoV-2 Spike S1 Protein (hFc) | SARS-CoV-2 | HEK293 | ||
The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike is essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. 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. It's been reported that SARS-CoV-2 (COVID-19 coronavirus, 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. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.
|
|||||
TMPY-06145 | SARS-CoV-2 Nucleocapsid Protein (E378Q, His) | SARS-CoV-2 | E. coli | ||
Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. The coronavirus N protein is required for coronavirus RNA synthesis and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is the most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to the formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of the N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.
|