目录号 | 产品详情 | 靶点 | |
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T36489 | |||
Malformin A is a cyclopentapeptide fungal metabolite that has been found in A. niger and has diverse biological activities. It is a plant growth regulator that induces malformations in plant structure. Malformin A inhibits replication of tobacco mosaic virus (TMV) in local lesion and leaf-disc assays (IC50s = 19.7 and 45.4 μg/ml, respectively). It is cytotoxic to NCI-H460, MIA PaCa-2, MCF-7, SF-268, and WI-38 cancer cells (IC50s = 70, 50, 100, 70, and 100 nM, respectively), inhibits proliferation of PC3 and LNCaP cells (IC50s = 130 and 90 nM, respectively), and induces apoptosis and necrosis in PC3 and LNCaP cells. Malformin A also increases the accumulation of reactive oxygen species, decreases the mitochondrial membrane potential, and induces autophagy in PC3 and LNCaP cells. It is toxic to mice when administered intraperitoneally (LD50 = 3.1 mg/kg) but not orally up to doses of 50 mg/kg. | |||
TP2182 | Others | ||
Lamin fragment has a peptide sequence of Lys-Ala-Gly-Gln-Val-Val-Thr-Ile-Trp. Lamin polypeptides have an almost complete α-helical conformation with multiple α-helical domains separated by non-α-helical linkers that are highly conserved in length and amin | |||
T60488 | |||
Ganciclovir (BW 759) hydrate 是一种核苷类似物,是具有口服活性的抗病毒剂,显示出抗巨细胞病毒活性。Ganciclovir hydrate 对疱疹病毒和其他一些 DNA 病毒也具有体外抗病毒活性。Ganciclovir hydrate 在体外抑制人类疱疹病毒 (HSV 1 型和 2 型,CMV) 和腺病毒血清型1、2、4、6、8、10、19、22 和 28 的复制。Ganciclovir hydrate 对猫疱疹病毒 1 型 (FHV-1) 的 IC50为 5.2 μM,可扩散到大脑。 | |||
T83854 | |||
BRC4wt是一种从人类BRCA2的BRC4重复区(1521-1536)衍生而来的乙酰化肽,并且是BRCA2与RAD51之间的蛋白质-蛋白质相互作用的抑制剂。当与阳离子穿膜肽(Arg)9结合时,BRC4wt缩短了体外DNA复制轨迹长度,并降低了由DNA拓扑异构酶I抑制剂坎普特西汀引起的DNA损伤的同源修复频率,同时也增强了聚(ADP-核糖)聚合酶(PARP)抑制剂奥拉帕尼在HeLa人类宫颈癌细胞和U2OS人类骨肉瘤细胞中诱导的细胞死亡,但在非癌症细胞hTERT RPE-1、MRC-5或MCF-10A中则不然。 | |||
T83706 | |||
BMAP 28是一种合成抗菌肽,对应牛防御素-5的132-158氨基酸。对大肠杆菌(E. coli)、金黄色葡萄球菌(S. aureus)、耐甲氧西林金黄色葡萄球菌(MRSA)、表皮葡萄球菌(S. epidermidis)及白色念珠菌(C. albicans)具有活性(MICs分别为2、2、4、1和8 µM)。在200 nM浓度下,BMAP 28能够使大肠杆菌的内膜渗透。在5 µM浓度下,减少Vero 76细胞中单纯疱疹病毒1型(HSV-1)的复制。在30 µM浓度下,对分离的人类红细胞引起溶血,并对分离的人类嗜中性粒细胞具有细胞毒性。BMAP 28 (0.8 mg/kg)可提高大肠杆菌或MRSA感染的小鼠的生存率,但对铜绿假单胞菌(P. aeruginosa)感染的小鼠无效。 | |||
T83693 | |||
Magainin 2是一种从非洲爪蟾(X. laevis)皮肤中分离出的阳离子肽,具有宿主防御和抗菌活性。该化合物对细菌E. coli、K. pneumoniae、S. epidermidis、S. aureus及真菌C. albicans表现出活性(MICs分别为5、10、10、50和80 µg/ml)。Magainin 2(20 µM)能降低猕猴桃花粉的萌发率和平均管长。在被单纯疱疹病毒1型(HSV-1)或2型(HSV-2)感染的Vero细胞中,它可减少病毒复制(EC50s分别为22.16和19.8 µM),同时不影响细胞活性,其50%细胞毒性浓度值(CC50)大于100 µM。 | |||
T36701 | |||
Phosphoramide mustard cyclohexanamine is the major metabolite for Cyclophosphamide , with anticancer activitiy. Phosphoramide mustard cyclohexanamine induces DNA adduct formation in ovarian granulosa cells, induces DNA damage and elicits the ovarian DNA repair response[1][2]. Phosphoramide mustard cyclohexanamine causes cytotoxicity through forming cross-linked DNA adducts which inhibit DNA strand separation during replication[1].Phosphoramide mustard cyclohexanamine destroys rapidly dividing cells by forming NOR-G-OH, NOR-G and G-NOR-G adducts with DNA, potentially leading to DNA damage[1].Phosphoramide mustard cyclohexanamine (3-6 μM; 48 hours) reduces cell viability in rat spontaneously immortalized granulosa cells (SIGCs)[1].Phosphoramide mustard cyclohexanamine (3-6 μM; 24-48 hours) induces DNA adduct formation[1].Phosphoramide mustard cyclohexanamine (3-6 μM; 24-48 hours) induces ovarian DNA damage in rat ovaries[1].Phosphoramide mustard cyclohexanamine increases DNA damage responses (DDR) gene (Atm, Parp1, Prkdc, Xrcc6, Brca1, Rad51) mRNA expression level[1].Phosphoramide mustard cyclohexanamine (3-6 μM; 24-48 hours) increased DDR proteins[1]. Cell Viability Assay[1] Cell Line: SIGCs Phosphoramide mustard cyclohexanamine (2.1-20.7 mg/kg; i.p.; daily; for 5 days) inhibits subcutaneous tumor growth in rats[2].Phosphoramide mustard cyclohexanamine (86.0 mg/kg; i.v.) has a plasma disappearance half-life of 15.1 minutes[2]. Animal Model: Rat, subcutaneously implanted Walker 256 carcinosarcoma tumor[2] [1]. Shanthi Ganesan, et al. Phosphoramide mustard exposure induces DNA adduct formation and the DNA damage repair response in rat ovarian granulosa cells. Toxicol Appl Pharmacol. 2015 Feb 1; 282(3): 252-258. [2]. S Genka, et al. Brain and plasma pharmacokinetics and anticancer activities of cyclophosphamide and phosphoramide mustard in the rat. Cancer Chemother Pharmacol. 1990;27(1):1-7. | |||
T36881 | |||
NHC-triphosphate triammonium is an active phosphorylated intracellular metabolite of β-d-N4-Hydroxycytidine (NHC) as a triphosphate form[1]. NHC-triphosphate triammonium is a weak alternative substrate for the viral polymerase and can be incorporated into HCV replicon RNA[1][2]. In an intracellular metabolism assay, HCV replicon cells are treated with 10 μM 3H-labeled NHC, and intracellular nucleotide levels are determined after 1, 2 and 8 hours incubations. NHC is rapidly convered into the mono-, di-, and triphosphate forms, and NHC-TP reaches up to 71.12 pM after 8 hours[1].NHC-triphosphate triammonium (NHC-TP) (5-40 μM) absence leads to full-length polymerization products, it can be a weak alternative substrate. In addition, incorporation of NHC-TP instead of CTP increases the molecular weight of the polymerization product by 16 (one extra oxygen) for each event and an obvious electrophoretic shift is observed in cell-free HCV NS5B polymerization reactions[1].Huh-7 cells are incubated with (10-50 μM; 4 h) NHC or a McGuigan phosphoramidate prodrug of NHC. Intracellular levels of the parental compounds and phosphorylated metabolites are measured using LC-MS/MS. Small amounts of NHC-monophosphate (MP) and NHC-diphosphate (DP) can be observed, while NHC-triphosphate triammonium remains the most abundant metabolite[2].NHC-triphosphate triammonium (NHC-TP) metabolite may directly target the viral polymerase and behave as a nonobligate chain terminator. It plays a prominent role in inhibiting early negative-strand RNA synthesis, either through chain termination or mutagenesis, which may in turn interfere with correct replicase complex formation. [1]. Stuyver LJ,et al. Ribonucleoside analogue that blocks replication of bovine viral diarrhea and hepatitis C viruses in culture.Antimicrob Agents Chemother. 2003 Jan;47(1):244-54. [2]. Maryam Ehteshami, et al. Characterization of β-d- N4-Hydroxycytidine as a Novel Inhibitor of Chikungunya Virus. | |||
T35701 | |||
FSL-1 TFA, a bacterial-derived toll-like receptor 2/6 (TLR2/6) agonist, enhances resistance to experimental HSV-2 infection[1]. FSL-1 TFA induces MMP-9 production through TLR2 and NF-κB/AP-1 signaling pathways in monocytic THP-1 cells[2]. FSL-1 significantly reduces HSV-2 replication in human vaginal epithelial cells (EC)[1].FSL-1 induces significant resistance to experimental genital HSV-2 infection through elaboration of a specific cytokine response profile[1].FSL-1 (50 ng/mL, 24 hours) induces MMP-9 expression at both mRNA and protein levels in human monocytic THP-1 cells[2].FSL-1 activates the MAP kinase/NF-κB signaling pathway[2]. Cell Viability Assay[1] Cell Line: V11I, V12I or V19I immortalized human vaginal EC FSL-1 application significantly protectes against genital HSV-2 challenge in mice[1]. Animal Model: Female Swiss-Webster mice (weighing 20-25 g)[1] [1]. William A Rose 2nd, et al. FSL-1, a bacterial-derived toll-like receptor 2/6 agonist, enhances resistance to experimental HSV-2 infection. Virol J. 2009 Nov 10;6:195. [2]. Cathryn J Kurkjian,et al. The Toll-Like Receptor 2/6 Agonist, FSL-1 Lipopeptide, Therapeutically Mitigates Acute Radiation Syndrome. Sci Rep. 2017 Dec 11;7(1):17355. | |||
T38174 | |||
Mpro inhibitor N3 hemihydrate is a potent inhibitor of SARS-CoV-2 Mpro with an EC50 of 16.77 μM for SARS-CoV-2. Mpro inhibitor N3 hemihydrate specifically inhibits Mpro from multiple coronaviruses, including SARS-CoV and MERS-CoV. Mpro inhibitor N3 hemihydrate displays inhibition against HCoV-229E, FIPV, and MHV-A59 with individual IC50 of 4.0 μM, 8.8 μM, and 2.7 μM, respectively[1][2]. Mpro inhibitor N3 hemihydrate (0-0.64 μM) is able to penetrate cells to inhibit the replication of IBV viruses, probably at the beginning of infection in embryos[3]. [1]. Jin Z, et al. Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors. Nature. 2020;582(7811):289-293.[2]. Yang H, et al. Design of wide-spectrum inhibitors targeting coronavirus main proteases [published correction appears in PLoS Biol. 2005 Nov;3(11):e428]. PLoS Biol. 2005;3(10):e324.[3]. Wang F, et al. Structure of Main Protease from Human Coronavirus NL63: Insights for Wide Spectrum Anti-Coronavirus Drug Design. Sci Rep. 2016;6:22677. Published 2016 Mar 7. |
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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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-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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TMPY-03955 | Influenza A H7N9 (A/Shanghai/2/2013) Nucleoprotein/NP Protein (His) | H7N9 | 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-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-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-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-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-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-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-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-04750 | CSNK2A2 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha', also known as CSNK2A2 and CK2A2, is a member of the protein kinase superfamily, Ser/Thr protein kinase family and CK2 subfamily. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. CSNK2A2 is a tetramer composed of an alpha chain, an alpha' and two beta chains. It is also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits. Ck2 is not a casein kinase in vivo, but over 1 substrates are known. The highly conserved amino acid sequences of its subunits and their broad expression suggest that Ck2 may have a fundamental role in cell function. Ck2 has been implicated in DNA replication, regulation of basal and inducible transcription, translation and control of metabolism. The Ck2alpha and Ck2alpha' isoforms (products of the genes Csnk2a1 and Csnk2a2, respectively) are highly homologous, the reason for their redundancy and evolutionary conservation is unknown. CSNK2A2 may be a candidate gene for these inherited syndromes.
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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-01674 | Human metapneumovirus (strain CAN97-83) Nucleoprotein/NP Protein (His & Myc) | HMPV | 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-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-01843 | Human parainfluenza 4b virus (HPIV-4b) Nucleoprotein/NP Protein (His) | HPIV-4b | E. coli | ||
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-01849 | Human parvovirus B19 (isolate AU) Non-capsid protein NS-1 (His & SUMO) | HPV B19 | E. coli | ||
Multifunctional protein essential for viral DNA replication, which cooperatively interacts with the viral DNA origin of replication and transactivates several promoters including the viral p6 promoter. Binds the origin of replication and performs an endonucleolytic nick within a conserved sequence in the viral genome, thereby initiating the rolling circle replication (RCR). Participates in the transcriptional regulation the viral p6 promoter that regulates all viral transcripts and the cellular CDN1A or IL6 promoters. Transactivates several host promoters some of which induce the S cell cycle phase for the production of host replicative proteins. Upregulates the expression of host E2F4 and E2F5 and interacts with both these factors thereby inhibiting the host cell cycle G2/M transition. This arrest promotes apoptosis for viral release.
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TMPH-00366 | Chicken anemia virus (isolate Germany Cuxhaven-1) Apoptin Protein (GST) | CAV | E. coli | ||
May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle.
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TMPH-01841 | Human parainfluenza 1 virus (HPIV-1) Nucleoprotein/NP Protein (His) | HPIV-1 | 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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TMPH-00524 | ATP-dependent DNA helicase dda Protein, Enterobacteria phage T4, Recombinant (His) | Enterobacteria phage T4 | 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-02550 | BLM Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
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-00365 | Chicken anemia virus (isolate USA 26p4) Apoptin Protein (His) | CAV | E. coli | ||
May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle.
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TMPH-01010 | BLM Protein, Human, Recombinant (His) | Human | E. coli | ||
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-00367 | Chicken anemia virus (isolate Germany Cuxhaven-1) Apoptin Protein (His & SUMO) | CAV | E. coli | ||
May act as transcriptional regulator. Induces apoptosis in infected cells. Element of infectious replication cycle.
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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-01829 | Human Papilloma Virus type 11 (HPV 11) Regulatory Protein E1 (His) | HPV 11 | 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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TMPH-00252 | Bovine coronavirus (strain Mebus) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00253 | Bovine coronavirus (strain 98TXSF-110-LUN) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00255 | Bovine coronavirus (strain LSU-94LSS-051) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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