目录号 | 产品详情 | 靶点 | |
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TN2283 | HIV Protease | ||
Tripterifordin 在 H9 淋巴细胞中显示出抗 HIV 复制活性,EC50值为 3100 nM。 | |||
T38514 | Others HIV Protease | ||
PMEDAP 是有效的人类免疫缺陷病毒 (HIV) 复制抑制剂。它具有抗小鼠巨细胞病毒活性。它有效抑制莫罗尼鼠肉瘤病毒诱导的肿瘤形成和相关死亡率。 | |||
T11539 | HCV Protease | ||
HCV-IN-29 是一种丙型肝炎病毒抑制剂。 | |||
T38237 | Nucleoside Antimetabolite/Analog HCV Protease | ||
2'-O-Methylcytidine 是 2'-代核苷,可抑制 HCV 复制。 它在体外抑制 NS5B 催化的 RNA 合成,其抑制方式是与底物核苷三磷酸竞争。 | |||
T11541 | Others HCV Protease | ||
HCV-IN-30 是 HCV NS5A 复制复合物的抑制剂(基因型 1a 和 1b 复制子的 IC50 = 901 和 102 nM)。 | |||
T1068 | Others DNA/RNA Synthesis | ||
Dithranol (cignoline) 是蒽醌衍生物,可破坏线粒体功能和结构,用于治疗皮肤病。 | |||
T14495 | Influenza Virus | ||
Baloxavir (S-033447) 是衍生自前药 Baloxavir marboxil,是流感病毒聚合酶 PA 亚基的一流帽依赖性核酸内切酶抑制剂。它抑制病毒 RNA 的转录和复制,具有强大的抗病毒活性。 | |||
T9212 | Others HIV Protease | ||
IMB-301是根据 hA3G 模型通过虚拟筛选的一种小分子抑制剂。 | |||
T8371 | Virus Protease SARS-CoV | ||
ML188是一种选择性非共价 SARS-CoV3CLpro 抑制剂,具有抗病毒活性,IC50为 1.5 μM。 | |||
T8354 | Nucleoside Antimetabolite/Analog Influenza Virus DNA/RNA Synthesis | ||
Triazavirin 是一种核酸的核苷类似物和抗病毒剂,通过抑制病毒 RNA 和 DNA 的合成以及基因组片段的复制而起作用。在流感传播阶段,它可作为保护剂。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04870 | Zika virus (ZIKV) (strain Zika SPH2015) ZIKV-NS1 protein (His) | ZIKV | HEK293 | ||
Zika virus NS1 antigen is one of seven non-structural proteins. NS1 is involved in RNA replication. The possible effects of NS1 on hosts include: localizes to host cell surface and secreted extracellularly, modulates signalling of the innate immune system, has possible damages to platelets and endothelial cells through anti-NS1 antibodies.
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TMPY-06058 | Influenza A H3N2 (A/Hong Kong/2671/2019) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06061 | Influenza B (B/Washington/02/2019) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-02617 | Influenza A H2N2 (A/Ann Arbor/6/1960) Nucleoprotein/NP Protein (His) | H2N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-02876 | Influenza A H1N1 (A/California/07/2009) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPJ-00779 | TNF alpha Protein, Rabbit, Recombinant | Rabbit | E. coli | ||
Tumor necrosis factor alpha (TNFα) is the prototypic ligand of the TNF superfamily. TNFα forms a homotrimer and functions by activating two types of receptors TNF-R1 (TNF receptor type 1,p55R) and TNF-R2 (TNF receptor type 2,p75R). TNFα is a pleiotropic cytokine that is capable to promote inflammation, to induce apoptotic cell death, and to inhibit tumorigenesis and viral replication. TNFα is a potent lymphoid factor that exerts cytotoxic effects on a wide range of tumor cells and certain other target cells.
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TMPY-06059 | Influenza A H1N1 (A/Guangdong-Maonan/SWL1536/2019) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-04688 | Influenza B (B/Florida/4/2006) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-00560 | Influenza A H3N2 (A/Aichi/2/1968) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06062 | Influenza B (B/Phuket/3073/2013) Nucleoprotein/NP Protein (His) | Influenza B | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-04274 | Influenza A H1N1 (A/Brevig Mission/1/1918) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06060 | Influenza A H1N1 (A/Hawaii/70/2019) Nucleoprotein/NP Protein (His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-01382 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Nucleoprotein/NP Protein (I116M, His) | H1N1 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-06057 | Influenza A H3N2 (A/Hong Kong/45/2019) Nucleoprotein/NP Protein (His) | H3N2 | Baculovirus-Insect Cells | ||
Influenza viral nucleoprotein (NP) plays a critical role in virus replication and host adaptation. Nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. The nucleocapsid is a complex of the viral nucleoprotein, RNA, and several other viral proteins. The nucleoprotein forms large, RNA-bound, helical filaments and acts as a scaffold for additional viral proteins.
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TMPY-01201 | Human cytomegalovirus (HCMV) Glycoprotein B/gB Protein (His) | CMV | HEK293 | ||
Cytomegalovirus (CMV) (human herpesvirus 5) glycoprotein B, also referred as CMV gB or gB, which belongs to the herpesviridae glycoprotein B family. It is a 97-amino acid glycoprotein encoded by the ORF of UL55. Cytomegalovirus Glycoprotein B protein is the most abundant component of the envelope, a target of neutralizing antibodies with at least two defined neutralizing epitopes and an essential replication component. Cytomegalovirus Glycoprotein B protein plays important roles in HCMV entry, cell-cell spread of internal virions, and fusion of infected cells. In addition, Cytomegalovirus Glycoprotein B protein is one envelope protein capable of heparin binding. It forms a physical association with host cell annexin II independent of the presence of calcium.
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TMPY-00811 | Human cytomegalovirus (HCMV) Glycoprotein B/gB Protein | CMV | HEK293 | ||
Cytomegalovirus (CMV) (human herpesvirus 5) glycoprotein B, also referred as CMV gB or gB, which belongs to the herpesviridae glycoprotein B family. It is a 97-amino acid glycoprotein encoded by the ORF of UL55. Cytomegalovirus Glycoprotein B protein is the most abundant component of the envelope, a target of neutralizing antibodies with at least two defined neutralizing epitopes and an essential replication component. Cytomegalovirus Glycoprotein B protein plays important roles in HCMV entry, cell-cell spread of internal virions, and fusion of infected cells. In addition, Cytomegalovirus Glycoprotein B protein is one envelope protein capable of heparin binding. It forms a physical association with host cell annexin II independent of the presence of calcium.
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TMPY-03758 | Vaccinia Virus B18R/B19R Protein (His) | VACV | Baculovirus-Insect Cells | ||
B18R is a type I interferon (IFN)-binding protein, which is encoded by the B18R open reading frame in the WR (Western Reserve) strain of vaccinia virus. It is also known as B19R in the Copenhagen strain of Vaccinia. B18R exists in a soluble and a membrane-bound form. As a type I IFN receptor, B18R has a broad species specificity. It has high affinity for human IFN-alpha and also binds rabbit, bovine, rat, pig, and mouse IFN-alpha and IFN-beta. It has been shown that secreted B18R binds to uninfected and infected cells. It presents at the cell surface and protects cells from the antiviral state induced by IFN-alpha and IFN-beta. Binding of soluble recombinant B18R protects cultured cells from IFN and allows vaccinia virus replication.
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TMPY-01827 | CD30/TNFRSF8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03423 | MERS-CoV Nucleocapsid Protein (His) | MERS-CoV | 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.
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TMPY-05766 | Human coronavirus (HCoV-NL63) Nucleocapsid Protein (His) | HCoV-NL63 | 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.
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TMPY-05775 | Human coronavirus (HCoV-229E) Nucleocapsid Protein (His) | HCoV-229E | 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.
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TMPY-05774 | Human coronavirus (HCoV-OC43) Nucleocapsid Protein (His) | HCoV-OC43 | 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.
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TMPY-05773 | Human coronavirus (HCoV-HKU1) Nucleocapsid Protein (His) | HCoV-HKU1 | 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.
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TMPY-02286 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Matrix protein 1/M1 Protein (His) | H1N1 | E. coli | ||
The Influenza virus matrix protein 1 (M1) is a matrix protein of the influenza virus. M1 protein has been shown to play a crucial role in virus replication, assembly, and budding. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. M1 consists of two domains connected by a linker sequence. The N-terminal domain has a multi-helical structure. The C-terminal domain also contains an alpha-helical structure. The M1 protein is the most abundant structural protein in influenza A virus particles. M1 protein of the influenza A virus plays multiple roles in virion assembly and infection. M1 protein was a candidate antigen for a broad-spectrum influenza virus vaccine and the adjuvant chitosan significantly improved the efficacy of the M1 vaccine.
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TMPY-03356 | IFN gamma Protein, Mouse, Recombinant | Mouse | HEK293 | ||
IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02827 | IFN gamma Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01714 | IFN gamma Protein, Human, Recombinant | Human | CHO | ||
IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-06983 | IFN gamma Protein, Human, Recombinant (E. coli) | Human | E. coli | ||
IFN gamma, also known as IFNG, is a secreted protein that belongs to the type II interferon family. IFN gamma is produced predominantly by natural killer and natural killer T cells as part of the innate immune response, and by CD4 and CD8 cytotoxic T lymphocyte effector T cells once antigen-specific immunity develops. IFN gamma has antiviral, immunoregulatory, and anti-tumor properties. IFNG, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons. The IFNG monomer consists of a core of six α-helices and an extended unfolded sequence in the C-terminal region. IFN gamma is critical for innate and adaptive immunity against viral and intracellular bacterial infections and tumor control. Aberrant IFN gamma expression is associated with some autoinflammatory and autoimmune diseases. The importance of IFN gamma in the immune system stems in part from its ability to inhibit viral replication directly, and most importantly from its immunostimulatory and immunomodulatory effects. IFNG also promotes NK cell activity.
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TMPY-01032 | CD299 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
C-type lectin domain family 4, member M, also known as DC-SIGNR and CLEC4M, is a type II integral membrane protein that is 77% amino acid identical to DC-SIGN, an HIV gp120-binding protein. Though the encoded gene located in the same chromosome, DC-SIGN is expressed solely on dendritic cells, while DC-SIGNR is predominantly found in liver sinusoidal endothelial cells and lymph node, as well as placental endothelium. DC-SIGNR exists as a homotetramer, and the tandem repeat domain, also called neck domain, mediates oligomerization. DC-SIGNR is regarded as a pathogen-recognition receptor involved in peripheral immune surveillance in liver, and probably mediates the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. DC-SIGNR appears to selectively recognize and bind many viral surface glycoproteins containing high mannose N-linked oligosaccharides in a calcium-dependent manner, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S, as well as the cellular adhesion protein ICAM3. DC-SIGNR has been thought to play an important role in establishing HIV infection by enhancing trans-infection of CD4(+)T cells in the regional lymph nodes. It may affect susceptibility to HIV infection by a mechanism that is different in females and males. DC-SIGNR can bind to hepatitis C virus (HCV), and its polymorphism might affect HCV loads supporting the concept that DC-SIGNR contributes to HCV replication efficacy.
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TMPY-01885 | Human RSV (B1) glycoprotein G/RSV-G Protein (His) | RSV | HEK293 | ||
Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 8-9 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities.
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TMPY-01082 | Human respiratory syncytial virus (RSV) (A, rsb1734) glycoprotein G/RSV-G Protein (95% Homology) (His) | RSV | HEK293 | ||
Human respiratory syncytial virus (HRSV) is the most common etiological agent of acute lower respiratory tract disease in infants and can cause repeated infections throughout life. It is classified within the genus pneumovirus of the family paramyxoviridae. Like other members of the family, HRSV has two major surface glycoproteins (G and F) that play important roles in the initial stages of the infectious cycle. HRSV G protein is a type II glycoprotein of 289-299 amino acids (depending on the virus strain) with a signal/anchor hydrophobic domain and is extensively modified by the addition of both N-and O-linked oligosaccharides to achieve the mature form of 8-9 kDa. The C-terminal ectodomain of the G protein has a central region and four cysteines which are conserved in all HRSV isolates and have been proposed as the putative receptor binding site. The G protein mediates attachment of the virus to the host cell membrane by interacting with heparan sulfate, initiating the infection. As similar to mucins in amino acid compositions, the RSV G protein can interact with host CX3CR1, the receptor for the CX3C chemokine fractalkine, and thus modulates the immune response and facilitate infection. Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors. Unlike the other paramyxovirus attachment proteins, HRSV-G lacks both neuraminidase and hemagglutinating activities.
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TMPH-01507 | HAPLN4 Protein, Human, Recombinant (His) | Human | E. coli | ||
Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication.
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TMPH-01658 | MAGEA4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPH-03082 | DEFB106A Protein, Pan troglodytes, Recombinant (His & KSI) | Chimpanzee | E. coli | ||
Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. After replication, the nucleocapsid is recruited to the host Golgi apparatus by glycoprotein Gn for packaging into virus particles.
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TMPH-03416 | Rift valley fever virus (RVFV) (strain ZH-548 M12) Nucleoprotein/NP Protein (His & SUMO) | RVFV | E. coli | ||
Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. After replication, the nucleocapsid is recruited to the host Golgi apparatus by glycoprotein Gn for packaging into virus particles.
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TMPH-00919 | MGAT4A Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction. Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks.
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TMPH-00484 | Cationic trypsin Protein, Canine, Recombinant (His & SUMO) | Canine | E. coli | ||
DNA helicase that stimulates viral DNA replication and recombination. Plays a role in T4 DNA replication initiation by selecting and activating DNA origins. Acts by dissociating and reassociating with the DNA molecule being unwound. Unwinds DNA as a monomer in a 5'-to-3' direction at a rate of 250 bp/s and can efficiently displace proteins from the DNA.
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TMPH-02295 | UAP1 Protein, Human, Recombinant (His) | Human | Yeast | ||
ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction. Recruited by the KHDC3-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks.
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TMPH-01647 | MMP-20 Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
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TMPJ-01448 | 3CLpro/3C-like Protease Protein, SARS-CoV-2, Recombinant (His) | 2019-nCoV | E. coli | ||
The viral main proteinase (M pro , also called 3CL pro ), which controls the activities of the coronavirus replication complex. It functions as a cysteine protease engaging in the proteolytic cleavage of the viral precursor polyprotein to a series of functional proteins required for coronavirus replication and is considered as an appealing target for designing anti-SARS agents.
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TMPJ-01449 | 3CLpro/3C-like Protease Protein, SARS-CoV-2, Recombinant | SARS-CoV-2 | E. coli | ||
The viral main proteinase (M pro , also called 3CL pro ), which controls the activities of the coronavirus replication complex. It functions as a cysteine protease engaging in the proteolytic cleavage of the viral precursor polyprotein to a series of functional proteins required for coronavirus replication and is considered as an appealing target for designing anti-SARS agents.
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TMPH-01656 | MAGEA12 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPJ-01399 | ASF1A Protein, Human, Recombinant (His, T7) | Human | E. coli | ||
Human Histone Chaperone ASF1A (ASF1A) belongs to the H3/H4 family of histone chaperone proteins. ASF1A is ubiquitously expressed in many cells and tissues, interacting with histones H3 and H4. ASF1A cooperates with Chromatin Assembly Factor 1 to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. In addition, ASF1A is necessary for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.
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TMPH-00488 | Glycoprotein hormones alpha chain Protein, Canine, Recombinant (His) | Canine | Yeast | ||
Important in genetic recombination, DNA repair, and replication. Possesses pairing and strand-transfer activity. Interacts with dda and gene 32 proteins.
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TMPH-02905 | TRPC1 Protein, Mouse, Recombinant (His) | Mouse | in vitro E. coli expression system | ||
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPY-05682 | SARS-CoV-2 Plpro/papain-like protease Protein (aa 1564-1880, His) | SARS-CoV-2 | 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.
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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.
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TMPH-01216 | DSG1 Protein, Human, Recombinant (His & Myc) | Human | in vitro E. coli expression system | ||
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
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TMPH-02906 | Sialidase-1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPH-03123 | Rhodopsin Protein, Pig, Recombinant (GST & His) | Sus scrofa (Pig) | E. coli | ||
Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two replication forks in the bidirectionally replicating molecule, effectively resulting in multiple rounds of replication from a single initiation event. Binds specifically to the FLP recognition target (FRT) site where it induces DNA to bend. Three types of bend exist. Type I is approximately 60 degrees and results from 1 FLP molecule binding to 1 symmetry element. Type II is >144 degrees and results from FLP molecules binding to symmetry elements a and b. Type III is approximately 65 degrees and results from FLP molecules binding to symmetry elements b and c.
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