目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T40732 | |||
TMPD dihydrochloride 是酶促转化氧化还原的活性底物和用于还原血红素过氧化物酶的电子供体。 | |||
T8002 | Lipoxygenase | ||
3-hydroxycoumarin 是一种 15-LOX-1的有效氧化还原抑制剂,近期被证明能保护海胆生殖细胞免受紫外线 B 的损伤。 | |||
T7545 | Others | ||
6-Aminonicotinamide 是一种竞争性 NADP+依赖性酶,是一种烟酰胺抗代谢药,葡萄糖 6-磷酸脱氢酶抑制剂 (Ki=0.46 μM)。 它干扰糖酵解,导致 ATP 耗竭,并与 DNA 交联化学疗法药物,如Cisplatin,协同杀死癌细胞。 | |||
T5692 | Others Endogenous Metabolite | ||
Pyrroloquinoline quinone 是氧化还原辅助因子,一种阴离子型氧化还原循环原醌。它是哺乳动物的必需营养素,对免疫功能很重要。它是从嗜甲基细菌的培养物中分离的,也存在于哺乳动物的组织。 | |||
T0223 | Apoptosis Antioxidant Reactive Oxygen Species | ||
Tetrahydroxyquinone (Tetroquinone) 是一种苯醌,是一种抗白内障剂,具有氧化还原活性。它可与半醌自由基一起参与氧化还原循环,导致活性氧形成。 | |||
T5693 | Others Endogenous Metabolite | ||
Pyrroloquinoline quinone disodium salt (Methoxatin disodium salt) 一种阴离子型氧化还原循环原醌,作为氧化还原辅助因子。它是从嗜甲基细菌的培养物中分离的,也存在于哺乳动物的组织。它是哺乳动物的必需营养素,对免疫功能很重要。 | |||
T7714 | Tyrosinase | ||
Temocapil 是一种酪氨酸激酶抑制剂。 | |||
T6698 | RAAS | ||
Temocapril hydrochloride (CS-622 HCl) 是血管紧张素转化酶 (ACE) 抑制剂。Temocapril HCl 能够用于充血性心力衰竭、急性心肌梗死、高血压、胰岛素抵抗和肾脏疾病的研究。 | |||
TD0103 | Others | ||
Safranin (Basic Red 2) 是一种经典的吩嗪染料,具有平面结构和阳离子电荷,能够轻易插入包括 DNA、蛋白质在内的生物大分子。它在学术领域被广泛用作光谱探针及指示剂,可作为金属离子浓度测定中的氧化还原指示剂。 | |||
TP1604L | Others | ||
Thioredoxin reductase peptide acetate(950890-23-0 free base) 对应于硫氧还蛋白还原酶 (TrxR) 中的 53–67 位残基,用于硫氧还蛋白还原酶研究。哺乳动物硫氧还蛋白还原酶 (TR) 催化硫氧还蛋白 (Trx) 的氧化还原活性二硫键的还原,并且在结构和谷胱甘肽还原酶的作用机制,除了 C 末端的 16 个氨基酸延伸部分含有一个罕见的连位硒硫键。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPJ-00464 | APE Protein, Human, Recombinant | Human | E. coli | ||
Apurinic-Apyrimidinic Endonuclease 1 (APE1) is required for efficient DNA base excision repair. When the DNA glycosylase remove the damaged bases, APE1 cleaves the AP site to allow resynthesis and ligation to complete repair. APE1 stimulates the DNA binding activity of many transcription factors, which participate in cancer promotion and progression. APE1 regulates the redox state of multiple transcription factors, such as c-Jun, c-Fos, NF-kB, p53. APEN is also involved in calcium-dependent down-regulation of PTH expression.
|
|||||
TMPY-00382 | Thioredoxin/TRX Protein, Mouse, Recombinant | Mouse | E. coli | ||
Thioredoxin, also known as ATL-derived factor, Surface-associated sulphydryl protein, SASP and TXN, is a nucleus, cytoplasm and secreted protein that belongs to the thioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
|
|||||
TMPY-02201 | Peroxiredoxin 6 Protein, Human, Recombinant (His) | Human | E. coli | ||
PRDX6, a member of antioxidant protein superfamily, plays an important role in oxidative stress, catabolism of lipids and phospholipid lipisomes. Peroxiredoxin 6 (PRDX6) is involved in redox regulation of the cell and is thought to be protective against oxidant injury. Peroxiredoxin 6 (PRDX6) is a bifunctional protein with both glutathione peroxidase (GPx) and iPLA2 activities,which are concomitantly increased with the expression of PRDX6. PRDX6 promoted lung tumor growth in an in vivo allograft model.
|
|||||
TMPY-02462 | Peroxiredoxin 5 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Peroxiredoxin-5, also known as Alu corepressor 1, Antioxidant enzyme B166, Liver tissue 2D-page spot 71B, Peroxisomal antioxidant enzyme, Thioredoxin peroxidase PMP20, Thioredoxin reductase, PRDX5 and ACR1, is cytoplasm protein that belongs to the peroxiredoxin 2 family. Peroxiredoxin-5 / PRDX5 reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Peroxiredoxin-5 / PRDX5 is involved in intracellular redox signaling. The Peroxiredoxins / Prx are a family of 25 kDa peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. The mammalian Peroxiredoxins / Prx family is divided into six groups ( PRDX1,PRDX2, PRDX3, PRDX4, PRDX5, PRDX6 ) on the basis of homology of amino acid sequences. They are located in the cytosol and play a role in the cell signaling system. All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression.
|
|||||
TMPY-02250 | Thioredoxin/TRX Protein, Human, Recombinant | Human | E. coli | ||
Thioredoxin, also known as ATL-derived factor, Surface-associated sulphydryl protein, SASP and TXN, is a nucleus, cytoplasm and secreted protein that belongs to the thioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
|
|||||
TMPY-02208 | Peroxiredoxin 5 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peroxiredoxin-5, also known as Alu corepressor 1, Antioxidant enzyme B166, Liver tissue 2D-page spot 71B, Peroxisomal antioxidant enzyme, Thioredoxin peroxidase PMP20, Thioredoxin reductase, PRDX5 and ACR1, is cytoplasm protein that belongs to the peroxiredoxin 2 family. Peroxiredoxin-5 / PRDX5 reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Peroxiredoxin-5 / PRDX5 is involved in intracellular redox signaling. The Peroxiredoxins / Prx are a family of 25 kDa peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. The mammalian Peroxiredoxins / Prx family is divided into six groups ( PRDX1,PRDX2, PRDX3, PRDX4, PRDX5, PRDX6 ) on the basis of homology of amino acid sequences. They are located in the cytosol and play a role in the cell signaling system. All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression.
|
|||||
TMPY-02084 | Thioredoxin 2/TRX2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Thioredoxin-2, also known as TXN2, MTRX and TRX2, is a member of the thioredoxin family. Tryparedoxins (TXN) are thioredoxin-related proteins which, as trypanothione:peroxiredoxin oxidoreductases, constitute the trypanothione-dependent antioxidant defense and may also serve as substrates for ribonucleotide reductase in trypanosomatids. Thioredoxin-2 / TXN2 contains one thioredoxin domain. It is widely expressed in adult (at protein level) and fetal tissues. Human Thioredoxin-2 / TXN2 is a small redox protein important in cellular antioxidant defenses, as well as in the regulation of apoptosis. Thioredoxin-2 / TXN2 has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential. Thioredoxin-2 / TXN2 could be involved in the resistance to anti-tumor agents. It possesses a dithiol-reducing activity. Thioredoxin-2 / TXN2 plays an important role in protecting the mitochondria against oxidative stress and in sensitizing the cells to ROS-induced apoptosis. Mammalian Thioredoxin-2 / TXN2 is a mitochondrial isoform of highly evolutionary conserved thioredoxins. Thioredoxins are small ubiquitous protein-disulfide oxidoreductases implicated in a large variety of biological functions.
|
|||||
TMPY-01276 | Peroxiredoxin 1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peroxiredoxin-1, also known as Thioredoxin peroxidase 2, Natural killer cell-enhancing factor A, PRDX1, and PAGA, is a member of the ahpC/TSA family. Peroxiredoxin-1 is constitutively expressed in most human cells. It is induced to higher levels upon serum stimulation in untransformed and transformed cells. Peroxiredoxins (PRDXs) are a family of antioxidant enzymes that are also known as scavengers of peroxide in mammalian cells. The overexpression of Peroxiredoxin-1, which is one of the peroxiredoxins that is a ubiquitously expressed protein, was related to a poor prognosis in several types of human cancers. Peroxiredoxin-1 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin and may play an important role in eliminating peroxides generated during metabolism. Peroxiredoxin-1 Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. The reduced Peroxiredoxin-1 expression is an important factor in esophageal squamous cancer progression and could serve as a useful prognostic marker.
|
|||||
TMPY-02372 | Peroxiredoxin 1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Peroxiredoxin-1, also known as Thioredoxin peroxidase 2, Natural killer cell-enhancing factor A, PRDX1, and PAGA, is a member of the ahpC/TSA family. Peroxiredoxin-1 is constitutively expressed in most human cells. It is induced to higher levels upon serum stimulation in untransformed and transformed cells. Peroxiredoxins (PRDXs) are a family of antioxidant enzymes that are also known as scavengers of peroxide in mammalian cells. The overexpression of Peroxiredoxin-1, which is one of the peroxiredoxins that is a ubiquitously expressed protein, was related to a poor prognosis in several types of human cancers. Peroxiredoxin-1 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin and may play an important role in eliminating peroxides generated during metabolism. Peroxiredoxin-1 Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. The reduced Peroxiredoxin-1 expression is an important factor in esophageal squamous cancer progression and could serve as a useful prognostic marker.
|
|||||
TMPY-02200 | Peroxiredoxin 2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Peroxiredoxin-2, also known as Natural killer cell-enhancing factor B, NKEF-B, Thiol-specific antioxidant protein, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, PRDX2 and NKEFB, is a cytoplasm protein that belongs to the ahpC / TSA family. Peroxiredoxin-2 / PRDX2 contains one thioredoxin domain. Peroxiredoxin-2 / PRDX2 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system. Peroxiredoxin-2 / PRDX2 is not able to receive electrons from glutaredoxin. It may play an important role in eliminating peroxides generated during metabolism. Peroxiredoxin-2 / PRDX2 might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. The Peroxiredoxins / Prx are a family of peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. The mammalian Peroxiredoxins / Prx family is divided into six groups (PRDX1,PRDX2, PRDX3, PRDX4, PRDX5, PRDX6) on the basis of homology of amino acid sequences. They are located in the cytosol and play a role in the cell signaling system. All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression.
|
|||||
TMPY-05169 | Peroxiredoxin 2 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Peroxiredoxin-2, also known as Natural killer cell-enhancing factor B, NKEF-B, Thiol-specific antioxidant protein, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, PRDX2 and NKEFB, is a cytoplasm protein that belongs to the ahpC / TSA family. Peroxiredoxin-2 / PRDX2 contains one thioredoxin domain. Peroxiredoxin-2 / PRDX2 is involved in redox regulation of the cell. It reduces peroxides with reducing equivalents provided through the thioredoxin system. Peroxiredoxin-2 / PRDX2 is not able to receive electrons from glutaredoxin. It may play an important role in eliminating peroxides generated during metabolism. Peroxiredoxin-2 / PRDX2 might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. The Peroxiredoxins / Prx are a family of peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. The mammalian Peroxiredoxins / Prx family is divided into six groups (PRDX1,PRDX2, PRDX3, PRDX4, PRDX5, PRDX6) on the basis of homology of amino acid sequences. They are located in the cytosol and play a role in the cell signaling system. All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression.
|
|||||
TMPY-03605 | Glutaredoxin 1/GRX1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Glutaredoxin-1, also known as GRX1 and GLRX, belongs to theglutaredoxin family. Glutaredoxinsare smallredoxenzymes that useglutathioneas a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. Glutaredoxin-1 functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Glutaredoxin-1 exists in either a reduced or an oxidized form. Glutaredoxins function as electron carriers in the glutathione-dependent synthesis ofdeoxyribonucleotidesby the enzymeribonucleotide reductase.
|
|||||
TMPH-00418 | Rubredoxin Protein, Clostridium pasteurianum, Recombinant (His & SUMO) | Clostridium pasteurianum | E. coli | ||
Snake venom serine protease that may act in the hemostasis system of the prey.
|
|||||
TMPH-00739 | Thioredoxin-1 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT.
|
|||||
TMPH-00016 | Ferredoxin Protein, Acetoanaerobium sticklandii, Recombinant (His & Myc) | Acetoanaerobium sticklandii | E. coli | ||
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
|
|||||
TMPH-03505 | Glutaredoxin 4/GrxD Protein, Shigella flexneri, Recombinant (His & SUMO) | Shigella flexneri | E. coli | ||
This Recombinant Shigella flexneri grxD protein was made through genetic engineering. By putting the grxD gene into the genetic material of E.coli cell, the E.coli could be used as factories or producers to make the desired grxD protein for research uses. The expression region of this protein is at 1-115aa. N-terminal 6xHis-SUMO tag was used in the expression process. The purity is 85%+ determined by SDS-PAGE. The cytosolic monothiol glutaredoxin GrxD plays a role in adaptation to iron starvation during infection. GrxD is repressed by the transcription factor SreA in iron replete conditions. During iron starvation, GrxD displays predominant nuclear localization. Downregulation of GrxD expression results in de-repression of genes involved in iron-dependent pathways and repression of genes involved in iron acquisition during iron starvation, but did not significantly affect these genes during iron sufficiency. GrxD displays protein-protein interaction with components of the cytosolic iron-sulfur cluster biosynthetic machinery, indicating a role in this process, and with the transcription factors SreA and HapX, which mediate iron regulation of iron acquisition and iron-dependent pathways. There is a GrxD-independent mechanism for sensing iron sufficiency by HapX. Inactivation of SreA suppresses the lethal effect caused by GrxD inactivation. Taken together, this study demonstrates that GrxD is crucial for iron homeostasis in A. fumigatus.
|
|||||
TMPH-02153 | Sulfiredoxin-1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
interacts with the host receptor. Mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis.; class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.; Stable signal peptide (SSP): cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.
|
|||||
TMPY-03407 | NQO1 Protein, Human, Recombinant (His) | Human | E. coli | ||
NQO1 gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 forms homodimers and reduces quinones to hydroquinones. NQO1's enzymatic activity prevents the one-electron reduction of quinones that results in the production of radical species. Mutations in the NQO1 gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of NQO1 has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized. Recent pharmacological research suggests the feasibility of genotype-directed redox chemotherapeutic intervention targeting NQO1 breast cancer, a common missense genotype encoding a functionally impaired NQO1 protein.
|
|||||
TMPH-01975 | Prothrombin 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.
|
|||||
TMPY-04022 | BOLA1 Protein, Human, Recombinant (His) | Human | E. coli | ||
BOLA1 is a mitochondrial protein that counterbalances the effect of L-buthionine-(S,R)-sulfoximine (BSO)-induced glutathione (GSH) depletion on the mitochondrial thiol redox potential. Furthermore, overexpression of BOLA1 nullifies the effect of BSO and S-nitrosocysteine on mitochondrial morphology. Conversely, knockdown of the BOLA1 gene increases the oxidation of mitochondrial thiol groups. Supporting a role of BOLA1 in controlling the mitochondrial thiol redox potential is that BOLA1 orthologs only occur in aerobic eukaryotes. A measured interaction of BOLA1with the mitochondrial monothiol glutaredoxin GLRX5 provides hints for potential mechanisms behind BOLA1's effect on mitochondrial redox potential.
|
|||||
TMPH-00421 | Phospholipase C Protein, Clostridium perfringens, Recombinant (His) | Clostridium perfringens | E. coli | ||
May be involved in a redox system involving ascorbic acid.
|
|||||
TMPH-00679 | Peptide deformylase Protein, E. coli O157:H7, Recombinant (His) | E. coli | Yeast | ||
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
|||||
TMPH-00031 | Aerolysin Protein, Aeromonas sobria, Recombinant (His & Myc) | Aeromonas sobria | E. coli | ||
These quantitative data support a model where 2-CysPrx and Cyp20-3, by interaction, form a redox-sensitive regulatory module in the chloroplast which is under control of the photosynthesis-linked stromal pH value, the redox state and additional stromal protein factor(s).[2-CysPrx] PMID: 26872837 Substitution of Cys for Ser at amino acid location 150 of the alpha-helix of 2-Cys Prx A regulates/enhances the dual peroxidase and chaperone enzymatic functions. [2-cysteine peroxiredoxin A] PMID: 26141131 BAS1 and SOB7 act redundantly with respect to light promotion of cotyledon expansion, repression of hypocotyl elongation and flowering time in addition to other phenotypes not regulated by light. PMID: 15773851
|
|||||
TMPY-05058 | TMX1 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
As a thiol-based tumor suppressor, TMX1 increases mitochondrial ATP production and apoptosis progression. TMX1 is the first example of a topology-specific client protein redox catalyst acting both in the folding and in the degradative pathways.
|
|||||
TMPH-02763 | Lithostathine-1/Reg1 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
Probable thiol-disulfide oxidoreductase that may participate in various redox reactions and act as chaperone under heat shock. May interact with HSP70 proteins through the TPR repeats.
|
|||||
TMPY-02043 | PARK7/DJ-1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Parkinson's disease locus DJ-1 (PARK7) is a differentially expressed transcript. DJ-1 plays a physiologic role in protection of erythroid cells from oxidant damage, a function unmasked in the context of oxidative stress. PARK7 belongs to the peptidase C56 family of proteins. It acts as a positive regulator of androgen receptor-dependent transcription. It may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death. Mutations in the DJ-1 gene are associated with rare forms of autosomal recessive early-onset Parkinson's disease (PD). DJ-1/p53 interactions contribute to apoptosis resistance in clonal myeloid cells and may serve as a prognostic marker in patients with myelodysplastic syndromes (MDS). DJ-1 regulates redox signaling kinase pathways and acts as a transcriptional regulator of antioxidative gene batteries. Therefore, DJ-1 is an important redox-reactive signaling intermediate controlling oxidative stress after ischemia, upon neuroinflammation, and during age-related neurodegenerative processes. Augmenting DJ-1 activity might provide novel approaches to treating chronic neurodegenerative illnesses such as Parkinson's disease and acute damage such as stroke.
|
|||||
TMPH-01972 | Proteoglycan 4 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.
|
|||||
TMPJ-01225 | PDILT Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein Disulfide-Isomerase-Like Protein of the Testis (PDILT) is a protein that belongs to the protein disulfide isomerase family. Human PDILT is synthesized as a 584 amino acid precursor that contains an 20 amino acid signal sequence and a 564 amino acid mature chain. PDILT contains 1 thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity. PDILT is an enzyme in the endoplasmic reticulum in eukaryotes. It is not a disulfide-linked homodimer. The PDILT protein can interacts with ERO1L and CLGN. PDILT probable redox-inactive chaperone involved in spermatogenesis.
|
|||||
TMPY-02433 | APE1/APEX1 Protein, Human, Recombinant (His) | Human | E. coli | ||
The enzyme is known to be a redox factor (Ref-1) stimulating DNA binding activity of AP-1 binding proteins such as Fos and Jun as well as a multifunctional DNA repair enzyme having 5' AP endonuclease, DNA 3' repair diesterase, 3'-5' exonuclease and DNA 3'-phosphatase activities.Although Apex mRNA was expressed ubiquitously, the levels varied significantly, suggesting organ- or tissue-specific expression of the Apex gene. The highest level was observed in the testis, relatively high levels in the thymus, spleen, kidney and brain, and the lowest level in the liver in rats. However, the present results suggested that APEX/Ref-1 gene product can interact with AP-1 binding proteins in brain, especially in the hippocampal formation, to regulate some brain functions by redox-activation.
|
|||||
TMPJ-00720 | TXNDC12 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Thioredoxin Domain-Containing Protein 12 belongs to the thioredoxin superfamily. In this family, proteins possess a thioredoxin fold with a consensus active-site sequence (CxxC) and have roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors. TXNDC12 is widely expressed in many tissues and contains one thioredoxin domain.
|
|||||
TMPH-03443 | GPX2 Protein, S. cerevisiae, Recombinant (His & Myc) | Saccharomyces cerevisiae | E. coli | ||
Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress. Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin). Involved in sporulation.
|
|||||
TMPH-03108 | GPX5 Protein, Pig, Recombinant (E. coli, His & Myc) | Sus scrofa (Pig) | E. coli | ||
Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress. Plays an important role in the oxidative stress-induced response in the presence of Ca(2+). Has peroxidase activity using preferentially thioredoxin as a reducing power. The redox state of the mitochondrial GPX2 is regulated by TRX1 and TRX2 (cytoplasmic thioredoxin), and by TRX3 (mitochondrial matrix thioredoxin). Involved in sporulation.
|
|||||
TMPJ-00934 | PRDX3 Protein, Human, Recombinant | Human | E. coli | ||
Thioredoxin-Dependent Peroxide Reductase Mitochondrial (PRDX3) is an enzyme that belongs to the AhpC/TSA family. Human and mouse PRDX3 genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Human PRDX3 protein has an antioxidant function and is localized in the mitochondrion. PRDX3 is involved in redox regulation of the cell. PRDX3 protects radical-sensitive enzymes from oxidative damage by a radical-generating system. It acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.
|
|||||
TMPY-02271 | TRXR1/TXNRD1 Protein, Human, Recombinant (aa 161-647, His) | Human | E. coli | ||
Thioredoxin reductase 1 (TXNRD1) which is a selenocysteine-containing protein is overexpressed in many malignancies. TXNRD1 plays a key role in regulating cell growth and transformation, and protects cells against oxidative damage. We investigated the association between TXNRD1 polymorphisms and ATDH susceptibility. Moreover, TXNRD1 is an essential selenium-containing enzyme involved in detoxification of reactive oxygen species (ROS) and redox signaling. And genetic variations in TXNRD1 favor the development of Drug-induced liver injury (DILI), which is the most common adverse drug reaction.
|
|||||
TMPJ-00826 | TXN Protein, Human, Recombinant (His) | Human | E. coli | ||
Thioredoxin (TXN) is a member of the Thioredoxin family. Thioredoxin exists as a disulfide-linked homodimer and contains one Thioredoxin domain. Thioredoxin is up-regulated by ionizing radiation. Thioredoxin participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin also plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide.
|
|||||
TMPJ-00666 | CLIC2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Chloride Intracellular Channel Protein 2 (CLIC2) is a critical component of all living cells; it regulatescellular traffic of Chloride ion and it can be inserted into membranes anf form chloride ion channels. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions, channel activity depends on the pH. CLIC2 is involved in regulating membrane potential and organic solute transport. CLIC2 modulates the activity of RYR2 and inhibits Calcium influx. CLIC2 can be detected in the adult brain, liver, lung, heart, stomach, spleen and testis. It is expressed in fetal liver and adult skeletal muscle. CLIC2 is a potential candidate for one of many diseases linked to Xq28.
|
|||||
TMPJ-01098 | PRDX4 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peroxiredoxin-4 (PRDX4) is a member of the AhpC/TSA family. PRDX4 is a cytoplasmic protein and contains one thioredoxin domain. PRDX4 exists in homodimer or heterodimer with PRDX1. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. In addition, PRDX4 is probably involved in redox regulation of the cell, regulating the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.
|
|||||
TMPJ-01404 | TMX2 Protein, Human, Recombinant (His) | Human | E. coli | ||
TMX2 is a single-pass type I membrane protein and contains 1 thioredoxin domain. Thioredoxin plays an important role in various cellular processes through redox regulation. The Molecular Cloning and characterization of one member of the thioredoxin superfamily, designated as TMX2.The TMX2 cDNA consists of 1644 nucleotides and contains an open reading frame encoding a protein of 372 amino acids with a predicted molecular mass of 42.5 kDa and an isoelectric point of 8.94. The TMX2 protein may possess an N-terminal signal peptide, a potential transmembrane domain, an Myb DNA-binding domain repeat signature, a thioredoxin consensus pattern, an endoplasmic reticulum (ER) membrane retention signal (KKXX-like motif), and a dileucine motif in the tail.
|
|||||
TMPY-04771 | CARKL Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
CARKL, also known as SHPK, is a nonprotein kinase of glucose metabolism. CARKL has weak homology to several carbohydrate kinases, a class of proteins involved in the phosphorylation of sugars as they enter a cell, inhibiting return across the cell membrane. CARKL catalyzes an orphan reaction in the pentose phosphate pathway, refocusing cellular metabolism to a high-redox state upon physiological or artificial downregulation. CARKL-dependent metabolic reprogramming is required for proper M1- and M2-like macrophage polarization and uncover a rate-limiting requirement for appropriate glucose flux in macrophage polarization.
|
|||||
TMPJ-00704 | SCO1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Protein SCO1 Homolog, Mitochondrial (SCO1) is a member of the SCO1/2 family. SCO1 has a homodimer structure. SCO1 is located in mitochondrion and is highly expressed in muscle, heart, and brain. It is characterized by high rates of Oxidative Phosphorylation (OxPhos). SCO1 is thought to play a important role in cellular copper homeostasis, mitochondrial redox signaling and insertion of copper into the active site of COX. The defects of SCO1 can result in Mitochondrial Complex IV Deficiency (MT-C4D). A disorder of the mitochondrial respiratory chain has heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs.
|
|||||
TMPY-03406 | NMNAT1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
NMNAT, also known as NMNAT1, is a member of the Nicotinamide-nucleotide adenylyltransferases. It is widely expressed with high levels in skeletal muscle, heart, liver, and kidney. NMNAT appears to have the ability to protect against axonal degeneration following mechanical or toxic insults. The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca(2+) signaling pathways. NMNAT enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.
|
|||||
TMPH-01570 | KLHDC3 Protein, Human, Recombinant (E. coli, His & Myc) | 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.
|
|||||
TMPH-00411 | BoNT/C Protein, Clostridium botulinum, Recombinant (His & SUMO) | Clostridium botulinum C phage | E. coli | ||
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
|
|||||
TMPH-01569 | KLHDC3 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
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.
|
|||||
TMPJ-01020 | GFER Protein, Human, Recombinant (His) | Human | E. coli | ||
GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1/ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.
|
|||||
TMPY-02890 | ERP27 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
ERP27 contains 1 thioredoxin domain and is a noncatalytic member of the protein disulfide isomerase family. Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. ERP27 is a widely expressed protein which localizes to the ER and may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase. ERP27 doesn't contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.
|
|||||
TMPY-01589 | Serpin B10 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have been identified.Mouse SerpinB1, also known as Peptidase inhibitor 1, PI-1, Bomapin and SERPINB1, is a nucleus and cytoplasm protein that belongs to the serpin family and Ov-serpin subfamily. SerpinB1 is expressed specifically in the bone marrow. SerpinB1 is a protease inhibitor that may play a role in the regulation of protease activities during hematopoiesis and apoptosis induced by TNF. SerpinB1 is a redox-sensitive nuclear serpin that augments proliferation or apoptosis of leukaemia cells, depending on growth factors availability. SerpinB1 may regulate protease activities in the cytoplasm and the nucleus.
|
|||||
TMPY-02299 | ALDH3A1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme that catalyzes the oxidation of various aldehydes. Certain types of epithelial tissues in mammals, especially those continually exposed to environmental stress (e.g., corneal epithelium), express ALDH3A1 at high levels and its abundance in such tissues is perceived to help to maintain cellular homeostasis under conditions of oxidative stress. Metabolic as well as non-metabolic roles for ALDH3A1 have been associated with its mediated resistance to cellular oxidative stress. Aldehyde dehydrogenase 1A1 (ALDH1A1) and ALDH3A1 are corneal crystallins. They protect inner ocular tissues from ultraviolet radiation (UVR)-induced oxidative damage through catalytic and non-catalytic mechanisms. Additionally, ALDH3A1 has been postulated to play a regulatory role in the corneal epithelium based on several studies that report an inverse association between ALDH3A1 expression and corneal cell proliferation. Aldehyde dehydrogenase 3A1 (ALDH3A1) plays an important role in many cellular oxidative processes, including cancer chemoresistance, by metabolizing activated forms of oxazaphosphorine drugs such as cyclophosphamide (CP) and its analogues, such as mafosfamide (MF), ifosfamide (IFM), and 4-hydroperoxycyclophosphamide (4-HPCP). Compounds that can selectively target ALDH3A1 could permit delineation of its roles in these processes and could restore chemosensitivity in cancer cells that express this isoenzyme. ALDH3A1 may act to protect corneal cells against cellular oxidative damage by metabolizing toxic lipid peroxidation products (e.g., 4-HNE), maintaining cellular GSH levels and redox balance, and operating as an antioxidant.
|
|||||
TMPH-01233 | DIP2C Protein, Human, Recombinant (His) | Human | Baculovirus | ||
Binds galactosides. Has high affinity for the Forssman pentasaccharide. Ligand for HAVCR2/TIM3. Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death. Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth. Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function. Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation. Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection. Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells. Inhibits degranulation and induces apoptosis of mast cells. Induces maturation and migration of dendritic cells. Inhibits natural killer (NK) cell function. Can transform NK cell phenotype from peripheral to decidual during pregnancy. Astrocyte derived galectin-9 enhances microglial TNF production. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion. Highly selective to the anion urate.; Acts as an eosinophil chemoattractant. It also inhibits angiogenesis. Suppresses IFNG production by natural killer cells.
|
|||||
TMPH-01609 | LGI1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles. In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex. In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes. The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes. May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region. Plays also an important role in the regulation of the innate immune response and antiviral cytosolic DNA sensing. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of proinflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling. Suppresses macrophage inflammatory response by blocking proinflammatory cytokine transcription and the induction of IL6. Binds to the proximity of proinflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the NRF2-binding motif and reactive oxygen species level. Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses. Once activated, limits the release of pro-inflammatory cytokines in response to human coronavirus SARS-CoV-2 infection and to virus-derived ligands through a mechanism that involves inhibition of IRF3 dimerization. Also inhibits both SARS-CoV-2 replication, as well as the replication of several other pathogenic viruses including Herpes Simplex Virus-1 and-2, Vaccinia virus, and Zika virus through a type I interferon (IFN)-independent mechanism.
|