目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T5705 | Dehydrogenase | ||
Glomeratose A 是分离自远志Polygala tenuifolia 中,是一种乳酸脱氢酶lactate dehydrogenase 抑制剂。 | |||
T15435 | Dehydrogenase | ||
GSK2837808A 是一种选择性的乳酸脱氢酶A 抑制剂,对 hLDHA (IC50:2.6 nM) 和 hLDHB (IC50:43 nM)。 | |||
T11829 | Dehydrogenase | ||
LDH-IN-1 是新型的基于吡唑的人乳酸脱氢酶抑制剂,对于 LDHA 和 LDHB 的 IC50 分别为32和27 nM。 | |||
T39280 | Others | ||
Nitrofen 是选择性接触除草剂,也是视原卟啉原氧化酶和网膜脱氢酶抑制剂。 | |||
T7835 | Dehydrogenase | ||
CM10是一种有效的乙醛脱氢酶 1A (ALDH1A) 家族选择性抑制剂,对于 ALDH1A1,ALDH1A2 和 ALDH1A3 的IC50分别为 1700、740 和 640 nM。CM 10 可以调节新陈代谢并具有抗癌活性。 | |||
T15827 | DHFR | ||
LY 345899 是叶酸的类似物,也是亚甲基四氢叶酸脱氢酶 (MTHFD1;DC301) 和MTHFD2抑制剂,其IC50值分别为 96 nM 和 663 nM,对MTHFD1的Ki=为 18 nM。 | |||
T15551 | Dehydrogenase | ||
IDH889 是可口服有效的,脑渗透性的,变构和突变特异性的异柠檬酸脱氢酶抑制剂,对 IDH1 R132* 突变型具有高效选择性。它高效抑制细胞内 2-HG 水平,IC50为 0.014 μM。 | |||
T7741 | Dehydrogenase Isocitrate Dehydrogenase (IDH) | ||
DS-1001b 是IDH-1(异柠檬酸脱氢酶-1) 突变体抑制剂。 | |||
TJS1382 | Dehydrogenase | ||
Taraxerone 是分离自景天的天然产物。它可以增强乙醇脱氢酶和乙醛脱氢酶活性,EC50分别为 512.42 μM 和 500.16 μM。 | |||
TQ0042 | Dehydrogenase Isocitrate Dehydrogenase (IDH) | ||
BAY-1436032 是一种选择性泛突变异柠檬酸脱氢酶 1 新型口服抑制剂。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-04180 | PfLDH Protein, P. falciparum, Recombinant (His) | P. falciparum | E. coli | ||
Plasmodium falciparum lactate dehydrogenase (PfLDH) is a key enzyme for energy generation of malarial parasites and is considered to be a potential antimalarial target. The ability of PfLDH- or PfIDEh-based immuno-PCR assays to detect <1 parasite/microL suggests that improvements of bound antibody sensor technology may greatly increase the sensitivity of malaria rapid diagnostic tests. The PfLDH test could be used to detect failures and, therefore, to assess anti-malarial efficacy.
|
|||||
TMPY-05357 | GCDH Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
GCDH Protein, Human, Recombinant (His) is expressed in Baculovirus-Insect Cells with His tag. The predicted molecular weight is 44.9 kDa. Accession number: Q92947-1
|
|||||
TMPH-02398 | ASA dehydrogenase Protein, Legionella pneumophila, Recombinant (His) | Legionella pneumophila | E. coli | ||
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
|
|||||
TMPH-00405 | Acyl-CoA dehydrogenase Protein, Clostridium acetobutylicum, Recombinant (His & Myc) | Clostridium acetobutylicum | E. coli | ||
Acyl-CoA dehydrogenase Protein, Clostridium acetobutylicum, Recombinant (His & Myc) is expressed in E. coli.
|
|||||
TMPY-03755 | Glycerol 3 Phosphate Dehydrogenase/GPD1 Protein, Human, Recombinant (His) | Human | E. coli | ||
GPD1 (Glycerol-3-Phosphate Dehydrogenase 1) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. GPD1 is a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. The encoded protein plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of dihydroxyacetone phosphate (DHAP) and reduced nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. It also reduces nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. Meanwhile, GPD1 and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria. Diseases associated with GPD1 include Hypertriglyceridemia, Transient Infantile, and Myopathy, Distal, 1.
|
|||||
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.
|
|||||
TMPY-02413 | Isocitrate dehydrogenase/IDH1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Isocitrate dehydrogenase/IDH1 Protein, Human, Recombinant (His) is expressed in E. coli with His tag. The predicted molecular weight is 48 kDa. Accession number: O75874
|
|||||
TMPY-02801 | PHGDH Protein, Human, Recombinant (His) | Human | E. coli | ||
PHGDH is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. This new family consists of D-isomer-stereospecific enzymes. The conserved residues in this family appear to be the residues involved in the substrate binding and the catalytic reaction, and thus to be targets for site-directed mutagenesis. A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. PHGDH catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor. Overexpression of PHGDH may cause certain breast cancers. Defects in PHGDH are the cause of phosphoglycerate dehydrogenase deficiency which is characterized by congenital microcephaly, psychomotor retardation, and seizures.
|
|||||
TMPJ-00524 | SORD Protein, Human, Recombinant (His) | Human | Human Cells | ||
Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyzes the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.
|
|||||
TMPJ-01075 | BDH1 Protein, Human, Recombinant (His) | Human | E. coli | ||
D-Beta-Hydroxybutyrate Dehydrogenase Mitochondrial (BDH) is a member of the short-chain dehydrogenases/reductases (SDR) family. BDH is localized in the mitochondrion matrix. BDH forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.
|
|||||
TMPY-02422 | PGD Protein, Human, Recombinant (His) | Human | E. coli | ||
PGD Protein, Human, Recombinant (His) is expressed in E. coli with His tag. The predicted molecular weight is 54.6 kDa. Accession number: P52209
|
|||||
TMPY-04241 | LDHA Protein, Rat, Recombinant (His) | Rat | E. coli | ||
LDHA (Lactate Dehydrogenase A) is a Protein Coding gene. The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA, a key enzyme regulating aerobic glycolysis, belongs to the lactate dehydrogenase family and is overexpressed in many human cancers, and correlates with poor clinical outcomes. LDHA can promote the Warburg effect to produce lactate and Adenosine Triphosphate (ATP) in aerobic conditions, which contributes to oncogenesis metastasis and drug resistance in various cancers. Up-regulation of lactate dehydrogenase LDHA is a frequent event in human malignancies and relate to poor postoperative outcome. Diseases associated with LDHA include Fanconi-Bickel Syndrome and Myoglobinuria.
|
|||||
TMPH-00917 | ADH4 Protein, Human, Recombinant (GST) | Human | E. coli | ||
ADH4 Protein, Human, Recombinant (GST) is expressed in E. coli.
|
|||||
TMPH-00912 | ADH5 Protein, Human, Recombinant (GST) | Human | E. coli | ||
ADH5 Protein, Human, Recombinant (GST) is expressed in E. coli.
|
|||||
TMPJ-00956 | MDH2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Malate dehydrogenase, mitochondrial is a 338 amino acids protein that belongs to the LDH/MDH superfamily. MDH type 1 family. MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. MDH2 is localized to the mitochondria and takes part in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH2 is highly expressed in the adrenal system, small intestine, heart and pancreas.
|
|||||
TMPH-00073 | ADH2 Protein, Arabidopsis thaliana, Recombinant (His) | Arabidopsis thaliana | E. coli | ||
Plays a central role in formaldehyde detoxification.
|
|||||
TMPH-00417 | 4HbD Protein, Clostridium kluyveri, Recombinant (His & Myc) | Clostridium kluyveri | E. coli | ||
4HbD Protein, Clostridium kluyveri, Recombinant (His & Myc) is expressed in E. coli.
|
|||||
TMPJ-00953 | ADH7 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Alcohol dehydrogenase class 4 mu/sigma chain (ADH7) is a cytoplasm enzyme which is a member of the alcohol dehydrogenase family. The expression of this gene makes it much more abundant in the stomach than the liver, thus it differs from the other known gene family members. ADH7 may participate in the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.
|
|||||
TMPJ-00463 | BDH2 Protein, Human, Recombinant (His) | Human | E. coli | ||
3-Hydroxybutyrate Dehydrogenase Type 2 belongs to the short-chain dehydrogenases/reductases (SDR) family. 3-Hydroxybutyrate Dehydrogenase Type 2 may play an important role in the peripheral utilization of 3-hydroxybutyrate. The cytoplasmic localization with its high ratio of oxidized NAD+, the NAD+ dependence and the kinetic parameters of 3-Hydroxybutyrate Dehydrogenase Type 2 make it suitable to conbert high levels of circulating 3-hydroxybutyrate into acetoacetate.
|
|||||
TMPH-00916 | ADH1B Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
ADH1B Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.
|
|||||
TMPJ-00955 | MDH1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Malate Dehydrogenase, Cytoplasmic (MDH1) is an enzyme which belongs to the MDH Type 2 sub-family of LDH/MDH superfamily. MDH1 is involved in the Citric Acid Cycle that catalyzes the conversion of Malate into Oxaloacetate (using NAD+) and vice versa. MDH1 should not be confused with Malic Enzyme, which catalyzes the conversion of Malate to Pyruvate, producing NADPH. MDH1 also participates in Gluconeogenesis, the synthesis of Glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by Pyruvate Carboxylase to form Pxaloacetate, a Citric Acid Cycle intermediate. In order to transport the Oxaloacetate out of the Mitochondria, Malate Dehydrogenase reduces it to Malate, and it then traverses the inner Mitochondrial membrane. Once in the cytosol, the Malate is oxidized back to Oxaloacetate by MDH1. Finally, Phosphoenol-Pyruvate Carboxy Kinase (PEPCK) converts Oxaloacetate to Phosphoenol Pyruvate.
|
|||||
TMPJ-00710 | ALDH1A2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Aldehyde dehydrogenase 1 family member A2 (ALDH1A2), also known as retinaldehyde dehydrogenase 2 (RALDH2), belongs to the aldehyde dehydrogenase family which contains two members, the ALDH1 s (ALDH1A1, ALDH1A2 and ALDH1A3) and the 9-cis retinaldehyde dehydrogenase ALDH8 s. ALDH1A2 is key enzyme that catalyzes the synthesis of retinoic acid (RA) from retinaldehyde. RA is a paracrine hormone signaling molecule that functions in developing and adult tissues. ALDH1A2 was also found to regulate normal and tumor cell growth and differentiation. Several studies showed that ALDH1A2 expression is increased after the appearance of AraC resistance in clinical cases which means this protein is effective in AraC resistance.
|
|||||
TMPH-02149 | ALDH5A1 Protein, Human, Recombinant (His) | Human | Yeast | ||
Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
|
|||||
TMPY-02599 | MDH1 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Malate dehydrogenases 1(MDH1 / MDHA) is a soluble form of malate dehydrogenases. Malate dehydrogenases (MDH) is a group of multimeric enzymes consisting of identical subunits usually organized as either dimer or tetramers with subunit molecular weights of 30-35 kDa. MDH has been isolated from different sources including archaea, eubacteria, fungi, plants, and mammals. MDH catalyzes the NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This reaction plays a key part in the malate/aspartate shuttle across the mitochondrial membrane, and in the tricarboxylic acid cycle within the mitochondrial matrix. The enzymes share a common catalytic mechanism and their kinetic properties are similar, which demonstrates a high degree of structural similarity. The three-dimensional structures and elements essential for catalysis are conserved between mitochondrial and cytoplasmic forms of MDH in eukaryotic cells even though these isoenzymes are only marginally related at the level of the primary structure.
|
|||||
TMPY-00506 | GAPDH Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH or G3PDH) is an enzyme of about 37kDa that is consisdered as a cellular enzyme involved in glycolysis. It catelyzes the sixth step of glycolysis. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a pleiotropic enzyme that is overexpressed in apoptosis and in several human chronic pathologies. Its role as a mediator for cell death has also been highlighted. A recent report suggests that GAPDH may be genetically associated with late-onset of Alzheimer's disease. Besides, deprenyl, which has originally been used as a monoamine oxidase inhibitor for Parkinson's disease, binds to GAPDH and displays neuroprotective actions.
|
|||||
TMPY-04568 | PDK1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Pyruvate dehydrogenase kinase, isozyme 1, also known as [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial and PDK1, is a member of the PDK / BCKDK protein kinase family. PDK-1 is expressed predominantly in the heart. It contains one histidine kinase domain. Pyruvate dehydrogenase kinase (PDK) isoforms are molecular switches that downregulate the pyruvate dehydrogenase complex (PDC) by reversible phosphorylation in mitochondria. An inhibitory effect of lipoic acid on PDKs would result in less phosphorylation of E1 and hence increased PDC activity. At least two isoenzymic forms of pyruvate dehydrogenase kinase ( PDK-1 and PDK-2 ) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation. PDK-3 appears to have the highest specific activity among the three isoenzymes. PDK-1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.
|
|||||
TMPY-04445 | PDK4 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
Pyruvate dehydrogenase kinase 4 (PDK4) is a mitochondrial protein that regulates the TCA cycle.PDK4, a vital mitochondrial protein, controls the switch between glycolysis and oxidative phosphorylation based upon nutrient availability.Pyruvate dehydrogenase kinase 4 (PDK4) mRNA has been reported as an up-regulated gene in the heart and skeletal muscle of carnitine-deficient juvenile visceral steatosis (JVS) mice under fed conditions. PDK4 plays an important role in the inhibition of glucose oxidation via the phosphorylation of pyruvate dehydrogenase complex (PDC).PDK4 gene expression is stimulated by thyroid hormone (T(3)), glucocorticoids, and long chain fatty acids.
|
|||||
TMPJ-00836 | G6PD Protein, Human, Recombinant (His) | Human | Human Cells | ||
Glucose-6-Phosphate 1-Dehydrogenase (G6PD) is a cytosolic enzyme that belongs to the glucose-6-phosphate dehydrogenase family. G6PD participates in the pentose phosphate pathway that supplies reducing energy to cells by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). G6PD produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power. NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. It is notable in humans that G6PD is remarkable for its genetic diversity. G6PD deficiency may cause neonatal jaundice, acute hemolysis, or severe chronic non-spherocytic hemolytic anemia.
|
|||||
TMPY-05066 | IVD Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
IVD (Isovaleryl-CoA Dehydrogenase) is a Protein Coding gene. IVD is a mitochondrial matrix enzyme that catalyzes the third step in leucine catabolism. IVD plays an essential role in processing proteins obtained from the diet. The body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for growth and development. Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine. Specifically, isovaleryl-CoA dehydrogenase is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy.
|
|||||
TMPY-00010 | LDHA Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
LDHA (Lactate Dehydrogenase A) is a Protein Coding gene. The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA, a key enzyme regulating aerobic glycolysis, belongs to the lactate dehydrogenase family and is overexpressed in many human cancers, and correlates with poor clinical outcomes. LDHA can promote the Warburg effect to produce lactate and Adenosine Triphosphate (ATP) in aerobic conditions, which contributes to oncogenesis metastasis and drug resistance in various cancers. Up-regulation of lactate dehydrogenase LDHA is a frequent event in human malignancies and relate to poor postoperative outcome. Diseases associated with LDHA include Fanconi-Bickel Syndrome and Myoglobinuria.
|
|||||
TMPY-00424 | HSD17B14 Protein, Human, Recombinant (His) | Human | HEK293 | ||
HSD17B14 Protein, Human, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 29.8 kDa. Accession number: A0A140VJH8
|
|||||
TMPH-02867 | ASPDH Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.
|
|||||
TMPH-02626 | DLAT Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
|
|||||
TMPY-02273 | 15-PGDH Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
15-hydroxyprostaglandin dehydrogenase [NAD+], also known as Prostaglandin dehydrogenase 1, HPGD, and PGDH1, is a member of the short-chain dehydrogenases/reductases (SDR) family. Prostaglandins (PGs) play a key role in the onset of labor in many species and regulate uterine contractility and cervical dilatation. Therefore, the regulation of prostaglandin output by PG synthesizing and metabolizing enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. HPGD is down-regulated by cortisol, dexamethasone, and betamethasone and down-regulated in colon cancer. It is up-regulated by TGFB1. HPGD contributes to the regulation of events that are under the control of prostaglandin levels. HPGD catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. and inhibits in vivo proliferation of colon cancer cells. Defects in HPGD are the cause of primary hypertrophic osteoarthropathy autosomal recessive (PHOAR), cranio-osteoarthropathy (COA), and isolated congenital nail clubbing.
|
|||||
TMPH-02625 | DLAT Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
|
|||||
TMPY-02446 | GAPDH Protein, Human, Recombinant (His) | Human | E. coli | ||
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH or G3PDH) is an enzyme of about 37kDa that is consisdered as a cellular enzyme involved in glycolysis. It catelyzes the sixth step of glycolysis. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a pleiotropic enzyme that is overexpressed in apoptosis and in several human chronic pathologies. Its role as a mediator for cell death has also been highlighted. A recent report suggests that GAPDH may be genetically associated with late-onset of Alzheimer's disease. Besides, deprenyl, which has originally been used as a monoamine oxidase inhibitor for Parkinson's disease, binds to GAPDH and displays neuroprotective actions.
|
|||||
TMPY-02799 | ALDH4A1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
ALDH4A1 is a member of the aldehyde dehydrogenase family. Aldehyde dehydrogenase enzymes function in the metabolism of many molecules including certain fats (cholesterol and other fatty acids) and protein building blocks (amino acids). Additional aldehyde dehydrogenase enzymes detoxify external substances, such as alcohol and pollutants, and internal substances, such as toxins that are formed within cells. ALDH4A1 is expressed abundantly in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas. It is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Defects in ALDH4A1 are the cause of hyperprolinemia type 2 (HP-2). HP-2 is characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
|
|||||
TMPY-01588 | ALDH7A1 Protein, Human, Recombinant (His) | Human | E. coli | ||
ALDH7A1 (Aldehyde dehydrogenase 7 family, member A1) is a member of subfamily 7 in the aldehyde dehydrogenase family. These enzymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. Mammalian ALDH7A1 is homologous to plant ALDH7B1 which protects against various forms of stress such as increased salinity, dehydration and treatment with oxidants or pesticides. In mammals, ALDH7A1 is known to play a primary role during lysine catabolism through the NAD+-dependent oxidative conversion of aminoadipate semialdehyde (AASA) to its corresponding carboxylic acid, α-aminoadipic acid. Deleterious mutations in human ALDH7A1 are responsible for pyridoxine-dependent and folinic acid-responsive seizures. ALDH7A1 is a novel aldehyde dehydrogenase expressed in multiple subcellular compartments that protects against hyperosmotic stress by generating osmolytes and metabolizing toxic aldehydes.
|
|||||
TMPJ-00834 | ACADM Protein, Human, Recombinant (His) | Human | E. coli | ||
Medium-Chain Specific Acyl-CoA Dehydrogenase (ACADM) is a mitochondrial fatty acid beta-oxidation that belongs to the acyl-CoA dehydrogenase family. ACADM is a homotetramer enzyme that catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. ACADM is specific for acyl chain lengths of 4 to 16. It is essential for converting these particular fatty acids to energy, especially during fasting periods. Defects in ACADM cause medium-chain acyl-CoA dehydrogenase deficiency, a disease characterized by hepatic dysfunction, fasting hypoglycemia, and encephalopathy, which can result in infantile death.
|
|||||
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-01225 | DHODH Protein, Human, Recombinant (His) | Human | E. coli | ||
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
|||||
TMPH-02850 | DHODH Protein, Mouse, Recombinant (His) | Mouse | in vitro E. coli expression system | ||
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
|||||
TMPH-01039 | CBR1 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione.
|
|||||
TMPJ-00962 | AKR1C3 Protein, Human, Recombinant (His) | Human | Human Cells | ||
AKR1C3, is an enzyme which belongs to the aldo/keto reductase family. It is expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. AKR1C3 catalyzes the conversion of aldehydes and ketones to alcohols. It catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2,which functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. It can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites.
|
|||||
TMPH-01202 | D2HGDH Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate. Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC). Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC.
|
|||||
TMPH-01040 | CBR1 Protein, Human, Recombinant (His) | Human | Yeast | ||
NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione.
|
|||||
TMPY-03433 | ALDH4A1 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
ALDH4A1 is a member of the aldehyde dehydrogenase family. Aldehyde dehydrogenase enzymes function in the metabolism of many molecules including certain fats (cholesterol and other fatty acids) and protein building blocks (amino acids). Additional aldehyde dehydrogenase enzymes detoxify external substances, such as alcohol and pollutants, and internal substances, such as toxins that are formed within cells. ALDH4A1 is expressed abundantly in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas. It is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Defects in ALDH4A1 are the cause of hyperprolinemia type 2 (HP-2). HP-2 is characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
|
|||||
TMPH-02627 | DHODH Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
|||||
TMPH-03278 | DHODH Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
|||||
TMPY-01264 | 15-PGDH Protein, Human, Recombinant (His) | Human | E. coli | ||
15-hydroxyprostaglandin dehydrogenase [NAD+], also known as Prostaglandin dehydrogenase 1, HPGD, and PGDH1, is a member of the short-chain dehydrogenases/reductases (SDR) family. Prostaglandins (PGs) play a key role in the onset of labor in many species and regulate uterine contractility and cervical dilatation. Therefore, the regulation of prostaglandin output by PG synthesizing and metabolizing enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. HPGD is down-regulated by cortisol, dexamethasone, and betamethasone and down-regulated in colon cancer. It is up-regulated by TGFB1. HPGD contributes to the regulation of events that are under the control of prostaglandin levels. HPGD catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. and inhibits in vivo proliferation of colon cancer cells. Defects in HPGD are the cause of primary hypertrophic osteoarthropathy autosomal recessive (PHOAR), cranio-osteoarthropathy (COA), and isolated congenital nail clubbing.
|