目录号 | 产品详情 | 靶点 | |
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T71849 | |||
STK683963 是细胞ATG4B 活性的强激活剂。STK683963 可以作为细胞中 ATG4B 氧化还原调节的介质。STK683963 可用于癌症研究。 | |||
T62910 | |||
Antibacterial agent 62 是一种新型氧化还原循环抗结核化合物,对生长和营养缺乏的表型耐药非生长细菌表现出显著的杀菌作用。 | |||
T80849 | |||
VU661, 一种吩嗪甲酰胺类化合物,作为昼夜节律调节剂能促使昼夜节律周期延长,该小分子具备氧化还原活性。 | |||
T76116 | |||
L-Lactate dehydrogenase (L-乳酸脱氢酶) 是一种氧化还原酶。L-Lactate dehydrogenase 在体内催化 NADH 将丙酮酸还原为 L-乳酸。 | |||
T31899 | |||
FY26 is a potent Os(II) anticancer drug candidate, exerts its activity by generating reactive oxygen species and disrupting the redox balance in cancer cells Coadministration of FY26 and nontoxic doses of L-BSO allows the potentiation of its anticancer ac | |||
T35981 | Antioxidant | ||
Biliverdin hydrochloride 是一种由血红素氧化形成的四吡咯水溶性化合物,具有潜在的抗氧化活性,参与胆绿素-胆红素氧化还原系统。 | |||
T36066 | |||
NADP+ is the oxidized form of the electron donor nicotinamide adenine dinucleotide phosphate . It serves as a cofactor in various biological reactions. In addition, the balance between these reduced and oxidized forms plays key roles in diverse cellular functions, including cell survival, the maintenance of redox status, and intracellular signaling. For example, binding of NADP+ to β-subunits of Kv channels activates ion transport, whereas NADPH stabilizes channel inactivation. NADP+ is biosynthesized from NAD+ by NAD kinase, with ATP as the phosphoryl donor. | |||
T37612 | |||
IBTP is a lipophilic cation that is accumulated in mitochondria and forms stable thioether adducts in a thiol-specific manner. As a result, mitochondrial proteins that have changed thiol redox state following oxidative stress are selectively tagged with IBTP and can be separated by two-dimensional electrophoresis and isolated. IBTP-tagged proteins can also be evaluated by immunoblotting using an antibody directed against the triphenylphosphonium moiety of the IBTP molecule. IBTP has also been used as a mitochondria-targeted soft electrophile to inhibit mitochondrial oxidative phosphorylation. | |||
T36173 | |||
Glutathione can occur in reduced (GSH), oxidized (GSSG), or in mixed disulfide forms and is ubiquitous in multiple biological systems serving as the major thiol-disulfide redox buffer of the cell. GSSG is the oxidized form of GSH . It can be reduced back to GSH through the NADPH-dependent enzyme glutathione reductase. GSSG functions as a hydrogen acceptor in the enzymatic determination of NADP+ and NADPH and can be a proximal donor in S-glutathionylation post translational modifications. The ratio of reduced glutathione to oxidized glutathione within cells is often used as an indicator of oxidative stress, with higher concentrations of GSSG predicting increased oxidative stress. | |||
T64076 | |||
Spermine Prodrug-1 是一种氧化还原敏感的精胺前药。Spermine Prodrug-1 对野生型 (CMS-24949) 和精胺合酶基因 (SMS) 突变型 (CMS-26559, 和 CMS-6233) 成纤维细胞具有抑制作用, 他们的 IC50 值分别为 326.7, 198.5, 和 244.1 μM。Spermine Prodrug-1 能够用于 Snyder Robinson 综合征的治疗。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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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.
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TMPY-00382 | Thioredoxin/TRX Protein, Mouse, Recombinant | Mouse | E. coli | ||
Thioredoxin/TRX Protein, Mouse, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 11.7 kDa and the accession number is P10639.
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TMPH-00739 | Thioredoxin-1 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin-1 Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 15.7 kDa and the accession number is P0AA25.
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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.
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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.
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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.
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TMPH-00418 | Rubredoxin Protein, Clostridium pasteurianum, Recombinant (His & SUMO) | Clostridium pasteurianum | E. coli | ||
Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Rubredoxin Protein, Clostridium pasteurianum, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 22.0 kDa and the accession number is P00268.
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TMPY-05169 | Peroxiredoxin 2 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus Insect Cells | ||
Peroxiredoxin 2 Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 24.1 kDa and the accession number is Q61171.
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TMPY-02200 | Peroxiredoxin 2 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
Peroxiredoxin 2 Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 24 kDa and the accession number is P32119.
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TMPY-02208 | Peroxiredoxin 5 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peroxiredoxin 5 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 18.5 kDa and the accession number is P30044-2.
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TMPY-01276 | Peroxiredoxin 1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Peroxiredoxin 1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 22.9 kDa and the accession number is A0A384NPQ2.
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TMPY-02372 | Peroxiredoxin 1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Peroxiredoxin 1 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 23.5 kDa and the accession number is P35700.
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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.
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TMPY-02462 | Peroxiredoxin 5 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Peroxiredoxin 5 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 18.5 kDa and the accession number is P99029-1.
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TMPY-02250 | Thioredoxin/TRX Protein, Human, Recombinant | Human | E. coli | ||
Thioredoxin/TRX Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 11.7 kDa and the accession number is P10599.
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TMPH-03505 | Glutaredoxin 4/GrxD Protein, Shigella flexneri, Recombinant (His & SUMO) | Shigella flexneri | E. coli | ||
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters.
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TMPH-02153 | Sulfiredoxin-1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.
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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.
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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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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.
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TMPY-05058 | TMX1 Protein, Human, Recombinant (mFc) | Human | HEK293 Cells | ||
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.
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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.
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TMPH-03073 | TDX Protein, Japonica rice, Recombinant (His & Myc) | Rice | 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. TDX Protein, Japonica rice, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 42.0 kDa and the accession number is Q6ES52.
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TMPJ-01225 | PDILT Protein, Human, Recombinant (His) | Human | HEK293 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.
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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.
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TMPJ-00720 | TXNDC12 Protein, Human, Recombinant (His) | Human | HEK293 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.
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TMPH-02195 | TXNDC17 Protein, Human, Recombinant (GST) | Human | E. coli | ||
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.
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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.
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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.
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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. GPX2 Protein, S. cerevisiae, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 23.4 kDa and the accession number is P38143.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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TMPY-02890 | ERP27 Protein, Human, Recombinant (mFc) | Human | HEK293 Cells | ||
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.
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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.
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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.
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