目录号 | 产品详情 | 靶点 | |
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T39868 | |||
Anticancer agent 11 an effective broad-spectrum anticancer agent, exerts its therapeutic potential by suppressing angiogenesis and facilitating the formation of DNA cross-links. | |||
T61046 | Apoptosis | ||
Anticancer agent 43 是一种有效的抗癌剂,通过 caspase 3, PARP1,Bax 蛋白依赖性途径诱导癌细胞凋亡 (apoptosis)。Anticancer agent 43 能够诱导 DNA 损伤,可用于研究大鼠胶质母细胞瘤 。 | |||
T60420 | DNA/RNA Synthesis | ||
Anticancer agent 73 是一种抗癌剂,它能有效地靶向反式激活反应(TAR)RNA 结合蛋白2(TRBP),并破坏TRBP-Dicer 的相互作用。Anticancer agent 73 通过调节 HCC 细胞中 miRNA 组和蛋白质组的表达谱,在体外和体内抑制 HCC 的生长和转移。 | |||
T60852 | |||
Anticancer agent 46是一种有效的抗癌剂, 在细胞实验中显示出抗增殖活性,对 MGC803细胞的 IC50为0.986μM。 | |||
T40330 | |||
Anticancer agent 15, an anticancer agent, exerts its efficacy by elevating intracellular levels of reactive oxygen species (ROS) and inducing cell death in melanoma cancer cells through necroptosis. | |||
T40479 | |||
Anticancer agent 13 is an anticancer agent from dicarboxylic acids and amines. | |||
T39501 | |||
Anticancer agent 7 (Example 5) is an anti-cancer agent that exhibits potent anticancer activity against H1650 lung cancer cells, with an IC50 value of 5 μM. | |||
T10331 | Others | ||
Anticancer agent 3 (Compound 4) is a anti-cancer agent. | |||
T27998 | |||
MDK-4204, an anticancer agent, shows significant anti-cancer activity with IC50 values of 8.8 µM and 9.5 µM in PC-3 and DU-145 cells, respectively. | |||
T62667 | |||
Anticancer agent 51 (compound 3d) 是一种有效的抗癌剂 (Ki: 731.62 nM),具有抗癌活性。Anticancer agent 51 具有潜力进行前列腺癌的研究。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-05033 | 5T4/TPBG Protein, Human, Recombinant (aa 60-345, His) | Human | HEK293 | ||
Trophoblast glycoprotein (TPBG), also known as 5T4, is the therapeutic target of several anticancer agents currently in clinical development, largely due to its high expression in tumors and low expression in normal adult tissues.
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TMPY-04644 | PDGFB Protein, Human, Recombinant (His) | Human | Yeast | ||
Platelet-derived growth factor-B (PDGFB) is necessary for normal cardiovascular development. The administration of PDGFB alone normalized tumor vasculature by increasing periendothelial coverage and vascular functionality. Interestingly, this effect exerted by PDGFB was also observed in the presence of DAPT. So PDGFB is able to improve tumor vascularity and allows the anticancer action of DAPT in the tumor.
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TMPY-06191 | 5T4/TPBG Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Trophoblast glycoprotein (TPBG), also known as 5T4, is the therapeutic target of several anticancer agents currently in clinical development, largely due to its high expression in tumors and low expression in normal adult tissues.
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TMPY-06214 | 5T4/TPBG Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Trophoblast glycoprotein (TPBG), also known as 5T4, is the therapeutic target of several anticancer agents currently in clinical development, largely due to its high expression in tumors and low expression in normal adult tissues.
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TMPY-06317 | 5T4/TPBG Protein, Human, Recombinant (aa 1-355, His) | Human | HEK293 | ||
Trophoblast glycoprotein (TPBG), also known as 5T4, is the therapeutic target of several anticancer agents currently in clinical development, largely due to its high expression in tumors and low expression in normal adult tissues.
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TMPY-05077 | PDGFB Protein, Rhesus, Recombinant (His) | Rhesus | Yeast | ||
Platelet-derived growth factor-B (PDGFB) is necessary for normal cardiovascular development. The administration of PDGFB alone normalized tumor vasculature by increasing periendothelial coverage and vascular functionality. Interestingly, this effect exerted by PDGFB was also observed in the presence of DAPT. So PDGFB is able to improve tumor vascularity and allows the anticancer action of DAPT in the tumor.
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TMPK-01310 | Syndecan-1 Protein, Rabbit, Recombinant (His) | Rabbit | HEK293 | ||
CD138 (syndecan-1, Sdc-1) is a member of the syndecan family that comprises heparan sulfate proteoglycans. CD138 is significant for cell-cell and cell-matrix interactions.CD138 plays a crucial role in carcinogenesis and is an attractive target for anticancer treatment with heparanase inhibitors and anti-CD138 antibodies for immunotherapy.
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TMPY-04877 | PDGFB Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Platelet-derived growth factor-B (PDGFB) is necessary for normal cardiovascular development. The administration of PDGFB alone normalized tumor vasculature by increasing periendothelial coverage and vascular functionality. Interestingly, this effect exerted by PDGFB was also observed in the presence of DAPT. So PDGFB is able to improve tumor vascularity and allows the anticancer action of DAPT in the tumor.
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TMPK-00721 | CX3CL1/Fractalkine Protein, Mouse, Recombinant (His & Avi), Biotinylated | Mouse | HEK293 | ||
Fractalkine/CX3C chemokine ligand 1 (CX3CL1) is a chemokine involved in the anticancer function of lymphocytes-mainly NK cells, T cells and dendritic cells. Its increased levels in tumors improve the prognosis for cancer patients, although it is also associated with a poorer prognosis in some types of cancers, such as pancreatic ductal adenocarcinoma.
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TMPY-02395 | PDGFB Protein, Cynomolgus, Recombinant (mFc) | Cynomolgus | HEK293 | ||
Platelet-derived growth factor-B (PDGFB) is necessary for normal cardiovascular development. The administration of PDGFB alone normalized tumor vasculature by increasing periendothelial coverage and vascular functionality. Interestingly, this effect exerted by PDGFB was also observed in the presence of DAPT. So PDGFB is able to improve tumor vascularity and allows the anticancer action of DAPT in the tumor.
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TMPY-05076 | PDGFB Protein, Canine, Recombinant (His) | Canine | Yeast | ||
Platelet-derived growth factor-B (PDGFB) is necessary for normal cardiovascular development. The administration of PDGFB alone normalized tumor vasculature by increasing periendothelial coverage and vascular functionality. Interestingly, this effect exerted by PDGFB was also observed in the presence of DAPT. So PDGFB is able to improve tumor vascularity and allows the anticancer action of DAPT in the tumor.
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TMPK-00060 | IL-17B Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
IL-17A, the prototypic member of the IL-17 family, several experimental findings strongly support the role of the IL-17B/IL-17 receptor B (IL-17RB) pathway in tumorigenesis and resistance to anticancer therapies. IL-17B/IL-17RB expression patterns and biological activities in cancer and highlight issues that remain to be addressed to better characterize IL-17B and its receptor as potential targets for enhancing the effectiveness of the existing cancer therapies.
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TMPK-00710 | Claudin-4 Protein-VLP, Human, Recombinant | Human | HEK293 | ||
Claudin-4 (CLDN4) is a key component of tight junctions (TJs) in epithelial cells. CLDN4 is overexpressed in many epithelial malignancies and correlates with cancer progression. Changes in CLDN4 expression have been associated with epigenetic factors (such as hypomethylation of promoter DNA), inflammation associated with infection and cytokines, and growth factor signaling. CLDN4 helps to maintain the tumor microenvironment by forming TJs and acts as a barrier to the entry of anticancer drugs into tumors.
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TMPH-01711 | ABCC1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export. Hydrolyzes ATP with low efficiency. Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation. Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthezing cells.
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TMPJ-00247 | METAP1 Protein, Human, Recombinant | Human | E. coli | ||
Methionine Aminopeptidase 1 is a member of the M24 family of metalloproteases. METAP1 plays an important role in G(2)/M phase regulation of the cell cycle and may serve as a promising target for the discovery and development of new anticancer agents. METAP1 and METAP2 have different substrate specificity due to the differences in both size and shape of the active sites. The proteolytic removal of N-terminal methionine from nascent peptides is catalyzed by a family of enzymes known as methionine aminopeptidases (MetAPs) and is essential for cell growth. Inhibition of METAPs provides a novel strategy in developing anti-cancer drugs.
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TMPY-00324 | METAP1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Processing of the N-terminal initiator methionine or formylated methionine is an essential cellular process conserved from prokaryotes to eukaryotes. The proteolytic removal of N-terminal methionine from nascent peptides is catalyzed by a family of enzymes known as methionine aminopeptidases (MetAPs) and is essential for cell growth. METAP1 and METAP2 have different substrate specificity due to the differences in both size and shape of the active sites. As a member of the M24 family of metalloproteases, METAP1 plays an important role in G(2)/M phase regulation of the cell cycle and may serve as a promising target for the discovery and development of new anticancer agents.
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TMPY-00883 | METAP1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Processing of the N-terminal initiator methionine or formylated methionine is an essential cellular process conserved from prokaryotes to eukaryotes. The proteolytic removal of N-terminal methionine from nascent peptides is catalyzed by a family of enzymes known as methionine aminopeptidases (MetAPs) and is essential for cell growth. METAP1 and METAP2 have different substrate specificity due to the differences in both size and shape of the active sites. As a member of the M24 family of metalloproteases, METAP1 plays an important role in G(2)/M phase regulation of the cell cycle and may serve as a promising target for the discovery and development of new anticancer agents.
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TMPY-01865 | BLMH Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
The papain superfamily member bleomycin hydrolase (BLMH) is a cytoplasmic cysteine peptidase that is highly conserved through evolution. The only known activity of the enzyme is metabolic inactivation of the glycopeptide bleomycin (BLM), an essential component of combination chemotherapy regimens for cancer. The papain superfamily member bleomycin hydrolase (BLMH) is a neutral cysteine protease with structural similarity to a 20S proteasome. Bleomycin (BLM), a clinically used glycopeptide anticancer agent. BLMH is an essential protectant against BLM-induced death and has an important role in neonatal survival and in maintaining epidermal integrity. Sequencing revealed several putative sites phosphorylated by different types of protein kinases, but no signal sequence, transmembrane domain, N-linked glycosylation site or DNA-binding motif.
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TMPY-04143 | Chemerin/RARRES2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Retinoic acid receptor responder protein 2 (RARRES2) is a small secreted protein involved in multiple cancers, including adrenocortical carcinoma (ACC). Serum RARRES2 may be used as a novel prognostic marker for ACC. Retinoic acid receptor responder 2 (RARRES2) is transcriptionally downregulated in multiple cancer types. Previous studies suggested that it can serve as an immune-dependent tumor suppressor by acting as a chemoattractant to recruit anticancer immune cells expressing its receptor, the chemerin chemokine receptor 1 (CMKLR1), to sites of tumor. Mechanistically, RARRES2 overexpression in ACC cells inhibited Wnt/beta-catenin pathway activity by promoting beta-catenin phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase. Thus RARRES2 is a novel tumor suppressor for ACC, which can function through an immune-independent mechanism.
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TMPY-00367 | Chemerin/RARRES2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Retinoic acid receptor responder protein 2 (RARRES2) is a small secreted protein involved in multiple cancers, including adrenocortical carcinoma (ACC). Serum RARRES2 may be used as a novel prognostic marker for ACC. Retinoic acid receptor responder 2 (RARRES2) is transcriptionally downregulated in multiple cancer types. Previous studies suggested that it can serve as an immune-dependent tumor suppressor by acting as a chemoattractant to recruit anticancer immune cells expressing its receptor, the chemerin chemokine receptor 1 (CMKLR1), to sites of tumor. Mechanistically, RARRES2 overexpression in ACC cells inhibited Wnt/beta-catenin pathway activity by promoting beta-catenin phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase. Thus RARRES2 is a novel tumor suppressor for ACC, which can function through an immune-independent mechanism.
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TMPY-02072 | HSF1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Heat shock factor protein 1, also known as heat shock transcription factor 1, HSF1, and HSTF1, is a cytoplasm and nucleus protein that belongs to the HSF family. HSF1 is the major transcription factor of HSPs (heat shock proteins) in response to various stresses. Wild type HSF1 (heat shock transcriptional factor 1) is normally inactive. HSF1 / HSTF1 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF1 / HSTF1 protects cells and organisms against various types of stress, either by triggering a complex response that promotes cell survival or by triggering cell death when stress-induced alterations cannot be rescued. HSF1 / HSTF1 is the key protein in regulating the stress response. It can be activated under heat, oxidative, or other stress conditions. Dominant-positive and dominant-negative HSF1 are two types of HSF1 mutants. Both of them gain DNA binding activity in the absence of stress. Also, dominant-positive HSF1 acquires transcriptional activity, which dominant-negative HSF1 does not acquire. HSF1 / HSTF1 was also reported to contribute to cell resistance against genotoxic stress, such as that caused by doxorubicin, an anticancer drug in common clinical use.
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TMPY-02076 | PIN1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peptidyl-prolyl cis-trans isomerase Pin1, also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Rotamase Pin1 and PIN1, peptidyl-prolyl cis/trans isomerase (PPIase), is a nucleus protein. PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and is presumed to operate as a molecular timer of this important process. PIN1 is an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. PIN1 displays a preference for an acidic residue N-terminal to the isomerized proline bond. Alterations in the level of PIN1 can influence hyperproliferative diseases such as cancer. PIN1 has been implicated in multiple aspects of cell cycle regulation. It has been suggested that PIN1 function is required for both normal mitotic progression and reentry into the cell cycle from quiescence. PIN1 is also a target of several oncogenic pathways and is overexpressed in human breast cancer. Its overexpression can lead to upregulation of cyclin-D1 and transformation of breast epithelial cells in collaboration with the oncogenic pathways. PIN1 plays a pivotal role in breast development and may be a promising new anticancer target. Pin1 activity regulates the outcome of proline-directed kinase (e.g. MAPK, CDK or GSK3) signalling and consequently regulates cell proliferation (in part through control of cyclin D1 levels and stability) and cell survival. Recent data also implicate Pin1 as playing an important role in immune responses, at least in part by increasing the stability of cytokine mRNAs by influencing the protein complexes to which they bind.
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TMPY-02114 | PIN1 Protein, Human, Recombinant | Human | E. coli | ||
Peptidyl-prolyl cis-trans isomerase Pin1, also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Rotamase Pin1 and PIN1, peptidyl-prolyl cis/trans isomerase (PPIase), is a nucleus protein. PIN1 is a peptidyl-prolyl isomerase that can alter the conformation of phosphoproteins and so affect protein function and/or stability. PIN1 regulates a number of proteins important for cell-cycle progression and is presumed to operate as a molecular timer of this important process. PIN1 is an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. PIN1 displays a preference for an acidic residue N-terminal to the isomerized proline bond. Alterations in the level of PIN1 can influence hyperproliferative diseases such as cancer. PIN1 has been implicated in multiple aspects of cell cycle regulation. It has been suggested that PIN1 function is required for both normal mitotic progression and reentry into the cell cycle from quiescence. PIN1 is also a target of several oncogenic pathways and is overexpressed in human breast cancer. Its overexpression can lead to upregulation of cyclin-D1 and transformation of breast epithelial cells in collaboration with the oncogenic pathways. PIN1 plays a pivotal role in breast development and may be a promising new anticancer target. Pin1 activity regulates the outcome of proline-directed kinase (e.g. MAPK, CDK or GSK3) signalling and consequently regulates cell proliferation (in part through control of cyclin D1 levels and stability) and cell survival. Recent data also implicate Pin1 as playing an important role in immune responses, at least in part by increasing the stability of cytokine mRNAs by influencing the protein complexes to which they bind.
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