目录号 | 产品详情 | 靶点 | |
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T12337L | Topoisomerase Antifungal | ||
Oxaquin TEA (MCB-3837 TEA) 是 MCB3681 的前体化合物,是一种 DNA 拓扑异构酶抑制剂,可用于研究梭菌感染和交叉感染。 | |||
T68132L | Adenosine Receptor | ||
Quercetin-3'-o-phosphate TEA (Quercetin 3'-phosphate TEA)是一种腺苷 A 受体拮抗剂,可用来预防和治疗代谢紊乱。 | |||
S00015 | Apoptosis Others Autophagy | ||
Tea polyphenol 也称为绿茶提取物,是茶中天然存在的酚类化合物,具有抗癌、抗氧化、抑制细胞增殖、诱导细胞凋亡、延缓细胞周期和调节致癌物代谢等生物活性。 | |||
T8361 | Potassium Channel | ||
Tetraethylammonium bromide (TEA bromide) 可以选择性阻断钾通道。 | |||
T36490 | |||
AZT triphosphate TFA (3'-Azido-3'-deoxythymidine-5'-triphosphate TFA) is a active triphosphate metabolite of Zidovudine (AZT). AZT triphosphate TFA exhibits antiretroviral activity and inhibits replication of HIV. AZT triphosphate TFA also inhibits the DNA polymerase of HBV. AZT triphosphate TFA activates the mitochondria-mediated apoptosis pathway[1][2][3]. Treatment with 100 μM Zidovudine (AZT) for 48h disrupts the mitochondrial tubular network via accumulation of AZT triphosphate (AZT-TP) in H9c2 cells. AZT triphosphate accumulation causes downregulation of Opa1 and upregulation of Drp1. AZT triphosphate causes mitochondrial dysfunction, increases the production of cytotoxic reactive oxygen species (ROS), and impairs the balance of the mitochondrial quality control system in H9c2 cell model established from rat embryonic myoblasts[1]. [1]. Ryosuke Nomura, et al. Azidothymidine-triphosphate Impairs Mitochondrial Dynamics by Disrupting the Quality Control System. Redox Biol. 2017 Oct;13:407-417. [2]. Takeya Sato, et al. Engineered Human tmpk/AZT as a Novel Enzyme/Prodrug Axis for Suicide Gene Therapy. Mol Ther. 2007 May;15(5):962-70. [3]. K Y Hostetler, et al. Enhanced Oral Absorption and Antiviral Activity of 1-O-octadecyl-sn-glycero-3-phospho-acyclovir and Related Compounds in Hepatitis B Virus Infection, in Vitro. Biochem Pharmacol. 1997 Jun 15;53(12):1815-22. | |||
T28615 | |||
Rp-cAMPS TEA salt is a cAMP-dependent protein kinase (PKA) activator. | |||
T20650 | |||
Triethanolamine oleate is a nonionic surfactant | |||
T34938 | |||
Triethanolamine linoleoyl glutamate is a bioactive chemical. | |||
T80977 | |||
TLR4agonist-1 (TEA) (compound 17a)为Toll-like Receptor 4 (TLR4)的高效激动剂,在RAW 264.7及MM6细胞中能有效促进MIP-1β的生成。 | |||
T41290 | Telomerase | ||
MST-312 (Telomerase Inhibitor IX) 是绿茶表没食子儿茶素没食子酸酯 (EGCG) 的衍生物。MST-312 是 telomerase 抑制剂,可用于肿瘤的研究,如多发性骨髓瘤 (MM)。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00541 | LON PROTEASE Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria.
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TMPK-01343 | 3CLpro/3C-like Protease Protein (A191T), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-04873 | Influenza A H10N7 (A/blue-winged teal/Louisiana/Sg-00073/2007) Hemagglutinin/HA Protein (His) | H10N7 | Baculovirus-Insect Cells | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPK-01335 | 3CLpro/3C-like Protease Protein (E166V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-01508 | Influenza A H5N2 (A/American green-winged teal/California/HKWF609/2007) Hemagglutinin/HA1 Protein (His) | H5N2 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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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-00680 | Protease 7 Protein, E. coli O157:H7, Recombinant (G236K K237G, His & SUMO) | E. coli | E. coli | ||
Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.
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TMPK-01338 | 3CLpro/3C-like Protease Protein (H172Y), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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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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TMPK-01341 | 3CLpro/3C-like Protease Protein (P132H), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01337 | 3CLpro/3C-like Protease Protein (Q189K), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-01543 | Influenza A H12N5 (A/green-winged teal/ALB/199/1991) Hemagglutinin/HA1 Protein (His) | H12N5 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPK-01340 | 3CLpro/3C-like Protease Protein (F140A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01345 | 3CLpro/3C-like Protease Protein (L50F, E166A, L167F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-01685 | Influenza A H5N2 (A/American green-winged teal/California/HKWF609/2007) Hemagglutinin/HA Protein (His) | H5N2 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPY-01542 | Influenza A H12N5 (A/green-winged teal/ALB/199/1991) Hemagglutinin/HA Protein (His) | H12N5 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPH-00902 | Human adenovirus C serotype 5 Protease (His & Myc) | HAdV-5 | E. coli | ||
Human adenovirus C serotype 5 Protease (His & Myc) is expressed in E. coli.
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TMPH-03056 | Vacuolar protease A Protein, Neosartorya fumigata, Recombinant (His) | Neosartorya fumigata | E. coli | ||
Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence.
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TMPH-00672 | Metalloprotease stcE Protein, E. coli O157:H7, Recombinant (His) | E. coli | E. coli | ||
Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes.
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TMPH-00781 | IGA1 protease Protein, Haemophilus influenzae, Recombinant (His & Myc) | Haemophilus influenzae | E. coli | ||
Virulence factor; cleaves host immunoglobulin A producing intact Fc and Fab fragments.
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TMPH-02225 | TEAD2 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3'). May be involved in the gene regulation of neural development. Binds to the M-CAT motif.
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TMPH-02222 | TEAD1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and cooperatively to the SPH and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription in vivo in a cell-specific manner. The activation function appears to be mediated by a limiting cell-specific transcriptional intermediary factor (TIF). Involved in cardiac development. Binds to the M-CAT motif.
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TMPH-03486 | Activin 1 Protein, Schmidtea mediterranea, Recombinant (His) | Schmidtea mediterranea | E. coli | ||
Activin 1 Protein, Schmidtea mediterranea, Recombinant (His) is expressed in E. coli with N-terminal 6xHis tag. The predicted molecular weight is 44.4 kDa. Accession number: U3RA98
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TMPK-01339 | 3CLpro/3C-like Protease Protein (S144A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01336 | 3CLpro/3C-like Protease Protein (L50F, E166V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01346 | 3CLpro/3C-like Protease Protein (L50F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-01027 | Mast Cell Protease-1/MCPT-1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Mast Cell Protease 1 (MMCP-1), also known as MCP-1, MCPT-1 and β-chymase, is a member of the Chymase family of chymotrypsin-like serine proteases. MCPT-1 is a 26 kDa β-chymase that is a component of mast cell granules. It is a 226 amino acid (aa) protein that has a conserved pattern of six cysteines and one potential glycosylation site. The granule-derived mouse mast cell proteases-1 and -2 (mMCP-1 and -2) colocalize in similar quantities in mucosal mast cells but micrograms of mMCP-1 compared with nanograms of mMCP-2 are detected in peripheral blood during intestinal nematode infection. mMCP-1 isolated from serum is complexed with serpins and both the accumulation and the longevity of mMCP-1 in the blood is due to complex formation, protecting it from a pathway that rapidly clears mMCP-2, which is unable to form complexes with serpins. The mucosal mast cell (MMC) granule-specific beta-chymase, mouse mast cell protease-1 (mMCP-1), is released systemically into the bloodstream early in nematode infection before parasite-specific IgE responses develop and TGF-beta1 induces the constitutive release of mMCP-1 by homologs of MMC in vitro. Expression of mMCP-1 is largely restricted to intraepithelial MMC and is thought to play a role in the regulation of epithelial permeability. Its activation is completed by the removal of a two residue N-terminal propeptide by a dipeptidyl peptidase (Cathepsin C). MCPT-1 is upregulated in the intestine in response to nematode infection, or systemic mucosa in response to anaphylaxis. Like human α-chymase, MCPT-1 is capable of the conversion of angiotensin I to angiotensin II, which plays a key role in the regulation of arterial pressure. The intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1.
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TMPH-02943 | TEAD4 Protein, Mouse, Recombinant | Mouse | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif. Might play a role in the embryonic development of skeletal muscle.
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TMPH-00767 | Gellan lyase Protein, Geobacillus stearothermophilus, Recombinant (His) | Geobacillus stearothermophilus | E. coli | ||
Cleaves the glycosidic bonds of gellan backbone and releases tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the non-reducing terminal. The enzyme is highly specific to the heteropolysaccharide gellan.
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TMPH-02226 | TEAD3 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to multiple functional elements of the human chorionic somatomammotropin-B gene enhancer.
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TMPH-02224 | TEAD4 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif.
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TMPH-02942 | TEAD4 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif. Might play a role in the embryonic development of skeletal muscle.
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TMPY-04851 | Influenza A H12N5 (A/green-winged teal/ALB/199/1991) Neuraminidase/NA | H12N5 | HEK293 | ||
Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies.
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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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TMPK-01342 | 3CLpro/3C-like Protease Protein (A191V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01347 | 3CLpro/3C-like Protease Protein (E166A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-04594 | Influenza A H10N7 (A/blue-winged teal/Louisiana/Sg-00073/2007) Hemagglutinin/HA1 Protein (His) | H10N7 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPK-01384 | SARS PLpro/papain-like protease Protein (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. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, 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.
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TMPJ-01431 | SARS-CoV-2 Papain-Like Protease Protein | SARS-CoV-2 | E. coli | ||
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.
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TMPK-01352 | SARS-CoV-2 PLpro/papain-like protease Protein (His & Avi) | 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. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, 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.
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TMPH-02223 | TEAD4 Protein, Human, Recombinant (His) | Human | E. coli | ||
Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds specifically and non-cooperatively to the Sph and GT-IIC 'enhansons' (5'-GTGGAATGT-3') and activates transcription. Binds to the M-CAT motif.
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TMPK-01344 | 3CLpro/3C-like Protease Protein (L167F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01348 | 3CLpro/3C-like Protease Protein, SARS-COV-2, Recombinant (aa 1-306) | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPY-00668 | APP/Protease nexin-II Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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TMPY-00323 | Hepatitis C virus (HCV-1a) NS3 protease/helicase immunodominant region Protein (aa 1356-1459, GST) | HCV | E. coli | ||
HCV NS3 displays three enzymatic activities: serine protease, NTPase, and RNA helicase. HCV NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A, and NS5A-NS5B. HCV NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. One of the HCV proteases, NS3-4A serine protease, is a non-covalent heterodimer consisting of a catalytic subunit (the N-terminal one-third of NS3 protein) and an activating cofactor (NS4A protein) and is responsible for cleavage at four sites of the HCV polyprotein.
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TMPY-05727 | SARS-CoV-2 3CLpro/3C-like protease Protein (His & Avi) | SARS-CoV-2 | E. coli | ||
3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site.
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TMPY-05752 | SARS-CoV-2 3CLpro/3C-like protease Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site.
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TMPH-00581 | ATP-dependent Clp protease adapter protein ClpS Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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TMPH-00717 | Protease 7 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.
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