目录号 | 产品详情 | 靶点 | |
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T36410 | |||
9(E),11(E),13(E)-Octadecatrienoic acid (β-ESA) is a conjugated polyunsaturated fatty acid that is found in plant seed oils and in mixtures of conjugated linolenic acids synthesized by the alkaline isomerization of linolenic acid. It reduces growth of Caco-2 colon cancer cells in a dose-dependent and time-dependent manner. In vitro, β-ESA induces DNA fragmentation and upregulation of pro-apoptotic Bax mRNA. β-ESA decreases protein expression of the apoptosis suppression factor Bcl-2 and induces apoptosis in T24 bladder cancer cells via production of reactive oxygen species. It also inhibits bacterial fatty acid dioxygenase with a Ki value of 49 nM in vitro. | |||
T83721 | |||
Hexafluoropropylene oxide dimer acid (HFPO-DA)作为一种全氟烷基醚羧酸(PFECA),于HepG2细胞中以250 µM的浓度使用时,可诱导凋亡并增加活性氧种类(ROS)的水平。HFPO-DA以每个蛋4 mg/kg的剂量,会减少孵化鸡右心室壁厚度,增加心率,并诱导肝脏脂肪积累,这些效应可通过敲除过氧化物酶体增殖物激活受体α(Ppara)基因编码实现预防。它减少了斑马鱼胚胎的存活百分比(LC50 = 7,651 mg/L)。在孕妇大鼠给药下,HFPO-DA(250 mg/kg)降低了新生大鼠的平均出生体重、存活时间和血清葡萄糖水平,并增加了血清胆固醇和甘油三酯水平。它已经被发现污染海水和河水。 | |||
T83768 | |||
Zofenoprilat是一种血管紧张素转换酶(ACE; IC50 = 8 nM for the rabbit lung enzyme)的抑制剂,同时也是前体药zofenopril的活性代谢产物。它能够抑制分离的豚鼠小肠中由血管紧张素I或缓激肽诱导的收缩(EC50s = 3 and 1 nM, respectively)。在人类脐静脉内皮细胞(HUVECs)中,Zofenoprilat (10 nM)降低基础内皮素-1分泌和一氧化氮(NO)生成,并阻止TNF-α诱导的活性氧种(ROS)增加以及谷胱甘肽(GSH)水平降低。Zofenoprilat (10 µM)保护初级人类心脏微血管内皮细胞免受多柔比星诱导的细胞毒性。此外,Zofenoprilat (10 µM)还能增加HUVECs中的硫化氢(H2S)生成,以及细胞的黏着、迁移和增殖。在以400 µM浓度使用时,它可以减少Langendorff分离的大鼠心脏灌流缺血再灌注损伤模型中的舒张末压和乳酸脱氢酶(LDH)释放。 | |||
TN3364 | Apoptosis Dehydrogenase p38 MAPK ROS JAK | ||
Agrimonolide 是一种来自异香豆素的化合物,主要存在于草药Agrimonia pilosa Ledeb 中,具有显著的生物活性。Agrimonolide 通过抑制脂多糖(LPS)诱导的JAK-STATs 和p38 MAPKs 信号通路的激活而发挥抗炎作用。Agrimonolide 及其衍生物去甲阿戈莫内德已显示出能够有效提高肝细胞中胰岛素介导的糖原水平,可能在调节胰岛素抵抗的HepG2细胞中发挥关键作用。Agrimonolide 通过靶向卵巢癌细胞中的SCD1,对癌症的进展和诱导细胞死亡和凋亡表现出抑制作用。特别是,Agrimonolide 对A2780和SKOV-3细胞的增殖、迁移和侵袭表现出剂量依赖性的抑制,同时促进细胞凋亡。该化合物还被发现能诱导铁介导的细胞死亡,同时增加活性氧(ROS)和总铁的水平。Agrimonolide 很容易穿过血脑屏障,表明其在神经系统疾病的治疗应用方面具有潜力。 | |||
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. | |||
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. | |||
T36176 | |||
AMK is an active metabolite of the neurohormone melatonin .1,2,3,4It is formed from melatoninviathe metabolic intermediate AFMK that is then deformylated by catalase or formamidase.5,6AMK scavenges singlet oxygenin vitrowhen used at a concentration of 200 μM.1It inhibits the epinephrine- and arachidonic acid-induced production of prostaglandin E2and PGD2in ovine seminal vesicle microsomes in a concentration- and time-dependent manner, as well as LPS-induced increases in COX-2 levels in RAW 264.7 macrophages when used at a concentration of 500 μM.2,3AMK (20 mg/kg) decreases MPTP-induced increases in lipid peroxidation in the cytosol and mitochondria from substantia nigra and striatum in a mouse model of MPTP-induced Parkinson’s disease.4 1.Schaefer, M., and Hardeland, R.The melatonin metabolite N1-acetyl-5-methoxykynuramine is a potent singlet oxygen scavengerJ. Pineal Res.46(1)49-52(2009) 2.Kelly, R.W., Amato, F., and Seamark, R.F.N-acetyl-5-methoxy kynurenamine, a brain metabolite of melatonin, is a potent inhibitor of prostaglandin biosynthesisBiochem. Biophys. Res. Commun.121(1)372-379(1984) 3.Mayo, J.C., Sainz, R.M., Tan, D.-X., et al.Anti-inflammatory actions of melatonin and its metabolites, N1-acetyl-N2-formyl-5-methoxykynuramine (AFMK) and N1-acetyl-5-methoxykynuramine (AMK), in macrophagesJ. Neuroimmunol.165(1-2)139-149(2005) 4.Tapias, V., Escames, G., López, L.C., et al.Melatonin and its brain metabolite N1-acetyl-5-methoxykynuramine prevent mitochondrial nitric oxide synthase induction in parkinsonian miceJ. Neurosci. Res.87(13)3002-3010(2009) 5.Tan, D.-X., Manchester, L.C., Reiter, R.J., et al.Melatonin directly scavenges hydrogen peroxide: A potentially new metabolic pathway of melatonin biotransformationFree Radic. Biol. Med.29(11)1177-1185(2000) 6.Hirata, F., Hayaishi, O., Tokuyama, T., et al.In vitro and in vivo formation of two new metabolites of melatoninJ. Biol. Chem.249(4)1311-1313(1974) |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-03553 | 15 Lipoxygenase 2 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
ALOX15B is a member of the lipoxygenase family of structurally related nonheme iron dioxygenases involved in the production of fatty acid hydroperoxides. ALOX15B converts arachidonic acid exclusively to 15S-hydroperoxyeicosatetraenoic acid, while metabolizing linoleic acid less effectively. ALOX15B gene is located in a cluster of related genes and a pseudogene that spans approximately 1 kilobases on the short arm of chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been described.
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TMPH-00026 | Catechol 1,2-dioxygenase Protein, Acinetobacter baylyi, Recombinant (His) | Actinia equina | E. coli | ||
Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.
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TMPY-03462 | 15 Lipoxygenase 2 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
ALOX15B is a member of the lipoxygenase family of structurally related nonheme iron dioxygenases involved in the production of fatty acid hydroperoxides. ALOX15B converts arachidonic acid exclusively to 15S-hydroperoxyeicosatetraenoic acid, while metabolizing linoleic acid less effectively. ALOX15B gene is located in a cluster of related genes and a pseudogene that spans approximately 1 kilobases on the short arm of chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been described.
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TMPY-01883 | EPOR Protein, Human, Recombinant (His) | Human | HEK293 | ||
Erythropoietin (EPO) is the major glycoprotein hormone regulator of mammalian erythropoiesis, and is produced by kidney and liver in an oxygen-dependent manner. The biological effects of EPO are mediated by the specific erythropoietin receptor (EPOR/EPO Receptor) on bone marrow erythroblasts, which transmits signals important for both proliferation and differentiation along the erythroid lineage. EPOR protein is a type â… single-transmembrane cytokine receptor, and belongs to the homodimerizing subclass which functions as ligand-induced or ligand-stabilized homodimers. EPOR signaling prevents neuronal death and ischemic injury. Recent studies have shown that EPO and EPOR protein may be involved in carcinogenesis, angiogenesis, and invasion.
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TMPY-02481 | ACOX1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Peroxisomal acyl-coenzyme A oxidase 1(ACOX1 or AOX) is the first enzyme of the fatty acid beta-oxidation pathway and belongs to the Acyl-CoA oxidase family. Human liver peroxisomes contain two acyl-CoA oxidases, namely, palmitoyl-CoA oxidase (ACOX1/AOX) and a branched chain acyl-CoA oxidase. The palmitoyl-CoA oxidase (ACOX1/AOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2. Human ACOX1/AOX is a protein of 661-amino acids, including the carboxyl-terminal sequence(Ser-Lys-Leu) known as a minimal peroxisome-targeting signal. Human ACOX1/AOX, the first and rate-limiting enzyme of the peroxisomal β-oxidation pathway, has two isoforms including ACOX1a and ACOX1b, transcribed from a single gene. The human ACOX1b isoform is more effective than the ACOX1a isoform in reversing the Acox1 null phenotype in the mouse partly because of the Substrate utilization differences.
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TMPY-03945 | Latent TGF beta 1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02638 | TGF beta 1 Protein, Human/Rhesus/Cynomolgus/Canine, Recombinant | Human,Rhesus,Cynomolgus,Canine | CHO | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01133 | Latent TGF beta 1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04211 | Latent TGF beta 1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00608 | TGF beta 1 Protein, Rat/Mouse, Recombinant | Mouse,Rat | HEK293 | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00500 | Latent TGF beta 1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
TGF-beta 1 is a member of the transforming growth factor beta (TGF-beta) family. The transforming growth factor-beta family of polypeptides are involved in the regulation of cellular processes, including cell division, differentiation, motility, adhesion and death. TGF-beta 1 positively and negatively regulates many other growth factors. It inhibits the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha and various interleukins. It can also decrease the expression levels of cytokine receptors. Meanwhile, TGF-beta 1 also increases the expression of certain cytokines in T cells and promotes their proliferation, particularly if the cells are immature. TGF-beta 1 also inhibits proliferation and stimulates apoptosis of B cells, and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells. As for myeloid cells, TGF-beta 1can inhibit their proliferation and prevent their production of reactive oxygen and nitrogen intermediates. However, as with other cell types, TGF-beta 1 also has the opposite effect on cells of myeloid origin. TGF-beta 1 is a multifunctional protein that controls proliferation, differentiation and other functions in many cell types. It plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Once cells lose their sensitivity to TGF-beta1-mediated growth inhibition, autocrine TGF-beta signaling can promote tumorigenesis. Elevated levels of TGF-beta1 are often observed in advanced carcinomas, and have been correlated with increased tumor invasiveness and disease progression.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-01318 | SOD3 Protein, Human, Recombinant | Human | E. coli | ||
Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
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TMPJ-00753 | Myoglobin Protein, Human, Recombinant (His) | Human | E. coli | ||
Myoglobin(MB) is a cytoplasmic protein expressed in myocytes of the heart and skeletal muscle that reversibly binds oxygen. It belongs to the globin family. Functions of myoglobin include oxygen storage and transport, as well as scavenging of NO and reactive oxygen species. MB serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Myoglobin also serves as a sensitive marker for muscle injury resulting from cardiac infarction. Surprisingly, mice in which myoglobin has been removed by gene targeting are able to perform extensive exercise and respond normally to hypoxic challenge.
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TMPH-01317 | SOD3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
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TMPH-00396 | TrhO Protein, Chlamydophila felis, Recombinant (His) | Chlamydia felis | E. coli | ||
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
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TMPH-03134 | Leghemoglobin Lb120-8 Protein, Pisum sativum, Recombinant (His) | Pisum sativum | E. coli | ||
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
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TMPH-03092 | Leghemoglobin A Protein, Phaseolus vulgaris, Recombinant (His & Myc) | Phaseolus vulgaris | E. coli | ||
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
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TMPH-01761 | Neuroglobin Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis.
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TMPH-00772 | Leghemoglobin C2 Protein, Glycine max, Recombinant (His) | Glycine max | E. coli | ||
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
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TMPJ-01248 | Cytoglobin/CYGB Protein, Human, Recombinant (His) | Human | E. coli | ||
Cytoglobin is a ubiquitously globin protein that belongs to the globin family. The highest expressed in heart, stomach, bladder and small intestine. CYGB acts a protector under conditions of oxidative stress. CYGB may be involved in intracellular oxygen storage or transfer, modulates oxygen and nitric oxide metabolism or scavenging free radicals within a cell.
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TMPH-02618 | CYP2E1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.
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TMPH-00575 | GlpD Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor.
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TMPH-03275 | Cytoglobin Protein, Rat, Recombinant (His & Myc) | Rat | E. coli | ||
May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. Plays a role in the development of liver fibrosis. Has a peroxidase activity.
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TMPH-02140 | CYP21A2 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
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TMPH-02141 | CYP21A2 Protein, Human, Recombinant (His) | Human | Yeast | ||
A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
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TMPJ-00800 | BPGM Protein, Human, Recombinant (His) | Human | E. coli | ||
Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.
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TMPH-01084 | CYP11A1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
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TMPH-02198 | TXNRD2 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis. Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
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TMPH-00099 | NDK1 Protein, Arabidopsis thaliana, Recombinant (His & Myc) | Arabidopsis thaliana | Yeast | ||
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Plays a role in response to reactive oxygen species (ROS) stress.
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TMPH-02233 | P4HTM Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
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TMPJ-01274 | ERO1L Protein, Human, Recombinant (His) | Human | Human Cells | ||
ERO1-Like Protein α (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It associates with ERP44, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport.
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TMPH-02617 | COX5A Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
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TMPH-01745 | NOX4 Protein, Human, Recombinant (Cell-Free, His) | Human | in vitro E. coli expression system | ||
Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.; Involved in redox signaling in vascular cells. Constitutively and NADPH-dependently generates reactive oxygen species (ROS). Modulates the nuclear activation of ERK1/2 and the ELK1 transcription factor, and is capable of inducing nuclear DNA damage. Displays an increased activity relative to isoform 1.
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TMPH-02106 | SH3PXD2A Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of amyloid-beta peptide.
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TMPH-01280 | EGLN1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.
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TMPH-02139 | CYP17A1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol (Probable). Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
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TMPK-00493 | OSMR Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
OSMR is targeted to the mitochondrial matrix via the presequence translocase-associated motor complex components, mtHSP70 and TIM44. OSMR interacts with NADH ubiquinone oxidoreductase 1/2 (NDUFS1/2) of complex I and promotes mitochondrial respiration. Deletion of OSMR impairs spare respiratory capacity, increases reactive oxygen species, and sensitizes BTSCs to IR-induced cell death.
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TMPH-01746 | NOX4 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Constitutive NADPH oxidase which generates superoxide intracellularly upon formation of a complex with CYBA/p22phox. Regulates signaling cascades probably through phosphatases inhibition. May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity. May regulate insulin signaling cascade. May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB. May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation. Isoform 3 is not functional. Isoform 5 and isoform 6 display reduced activity.; Involved in redox signaling in vascular cells. Constitutively and NADPH-dependently generates reactive oxygen species (ROS). Modulates the nuclear activation of ERK1/2 and the ELK1 transcription factor, and is capable of inducing nuclear DNA damage. Displays an increased activity relative to isoform 1.
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TMPK-00571 | OSMR Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
OSMR is targeted to the mitochondrial matrix via the presequence translocase-associated motor complex components, mtHSP70 and TIM44. OSMR interacts with NADH ubiquinone oxidoreductase 1/2 (NDUFS1/2) of complex I and promotes mitochondrial respiration. Deletion of OSMR impairs spare respiratory capacity, increases reactive oxygen species, and sensitizes BTSCs to IR-induced cell death.
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TMPH-01080 | Ceruloplasmin Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense.
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TMPH-02875 | ROMO1 Protein, Mouse, Recombinant (His) | Mouse | in vitro E. coli expression system | ||
Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage.; Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation.
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TMPY-01577 | ORP150 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Hypoxia up-regulated protein 1, also known as 15 kDa oxygen-regulated protein, 17 kDa glucose-regulated protein, ORP-15, GRP-17, and HYOU1, is a member of the heat shock protein 7 family. Seven members from four different heat shock protein (HSP) families were identified including HYOU1 (ORP15), HSPC1 (HSP86), HSPA5 (Bip), HSPD1 (HSP6), and several isoforms of the two testis-specific HSP7 chaperones HSPA2 and HSPA1L. HYOU1 is highly expressed in tissues that contain well-developed endoplasmic reticulum and synthesize large amounts of secretory proteins. It is highly expressed in the liver and pancreas. HYOU1 is also expressed in macrophages within aortic atherosclerotic plaques and in breast cancers. HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. Suppression of HYOU1 is associated with accelerated apoptosis. It is suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein is up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness.
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TMPH-02470 | PDK3 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species.
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TMPH-02104 | Sestrin-3/SESN3 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
May function as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway. May also regulate the insulin-receptor signaling pathway through activation of TORC2. This metabolic regulator may also play a role in protection against oxidative and genotoxic stresses. May prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein.
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TMPH-00359 | AlkB Protein, Caulobacter vibrioides, Recombinant (His & Myc) | Caulobacter vibrioides | E. coli | ||
Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents).
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TMPJ-00105 | SOD2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Superoxide Dismutase (SOD2) belongs to the iron/manganese superoxide dismutase family. SOD2 is a mitochondrial matrix protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 transforms toxic superoxide, a byproduct of the mitochondrial electron transport chain into hydrogen peroxide and diatomic oxygen. It is reported that oxidative stress plays an essential role in the development of breast cancer, while SOD2 is one of the primary enzymes that directly convert potential harmful oxidizing species to harmless metabolites.
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TMPY-02044 | SOD2 Protein, Human, Recombinant | Human | E. coli | ||
Superoxide dismutases (SOD) are important anti-oxidant enzymes that guard against superoxide toxicity. In humans, as in all mammals and most chordates, three forms of superoxide dismutase (SOD) are present: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular. Mitochondrial superoxide dismutase [SOD; manganese SOD (MnSOD) or SOD2] neutralizes highly reactive superoxide radical (O•-2), the first member in the plethora of mitochondrial reactive oxygen species.
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TMPH-03751 | CYBB Protein, Human, Recombinant (His) | Human | E. coli | ||
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. It is the terminal component of a respiratory chain that transfers single electrons from cytoplasmic NADPH across the plasma membrane to molecular oxygen on the exterior. Also functions as a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes. It participates in the regulation of cellular pH and is blocked by zinc.
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TMPJ-00946 | TALDO1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Transaldolase (TALDO1) belongs to the transaldolase family of Type 1 subfamily. TALDO1 is expressed selectively in oligodendrocytes of the brain. TALDO1 is a key enzyme of the nonoxidative pentose phosphate pathway providing ribose-5-phosphate for nucleic acid synthesis and NADPH for lipid biosynthesis. This pathway can also maintain glutathione at a reduced state and thus protect sulfhydryl groups and cellular integrity from oxygen radicals. TALDO1 deficiency results in telangiectases of the skin, hepatosplenomegaly and enlarged clitoris.
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TMPH-00577 | AlkB Protein, E. coli, Recombinant (His & Myc & SUMO) | E. coli | E. coli | ||
Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents).
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