Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| pyruvate dehydrogenase (acetyl-transferring) | Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12. Group: Enzymes. Synonyms: MtPDC (mitochondrial pyruvate dehydrogenase complex); pyruvate decarboxylase; pyruvate dehydrogenase; pyruvate dehydrogenase (lipoamide); pyruvate dehydrogenase complex; pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating); pyruvic acid dehydrogenase; pyruvic dehydrogenase. Enzyme Commission Number: EC 1.2.4.1. CAS No. 9014-20-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1217; pyruvate dehydrogenase (acetyl-transferring); EC 1.2.4.1; 9014-20-4; MtPDC (mitochondrial pyruvate dehydrogenase complex); pyruvate decarboxylase; pyruvate dehydrogenase; pyruvate dehydrogenase (lipoamide); pyruvate dehydrogenase complex; pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating); pyruvic acid dehydrogenase; pyruvic dehydrogenase. Cat No: EXWM-1217. |  |
| pyruvate dehydrogenase (NADP+) | The Euglena enzyme can also use FAD or methyl viologen as acceptor, more slowly. The enzyme is inhibited by oxygen. Group: Enzymes. Synonyms: pyruvate dehydrogenase (NADP). Enzyme Commission Number: EC 1.2.1.51. CAS No. 93389-35-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1155; pyruvate dehydrogenase (NADP+); EC 1.2.1.51; 93389-35-6; pyruvate dehydrogenase (NADP). Cat No: EXWM-1155. | |
| pyruvate dehydrogenase (quinone) | Flavoprotein (FAD). This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone. Does not accept menaquinone. Activity is greatly enhanced by lipids. Requires thiamine diphosphate. The enzyme can also form acetoin. Group: Enzymes. Synonyms: pyruvate dehydrogenase; pyruvic dehydrogenase; pyruvic (cytochrome b1) dehydrogenase; pyruvate:ubiquinone-8-oxidoreductase; pyruvate oxidase (ambiguous); pyruvate dehydrogenase (cytochrome) (incorrect). Enzyme Commission Number: EC 1.2.5.1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1220; pyruvate dehydrogenase (quinone); EC 1.2.5.1; pyruvate dehydrogenase; pyruvic dehydrogenase; pyruvic (cytochrome b1) dehydrogenase; pyruvate:ubiquinone-8-oxidoreductase; pyruvate oxidase (ambiguous); pyruvate dehydrogenase (cytochrome) (incorrect). Cat No: EXWM-1220. | |
| Native Rabbit Pyruvate Kinase/Lactic Dehydrogenase enzymes | Lactate dehydrogenase from rabbit muscle can be inhibited by ascorbate. Aldolase and actin were shown to block this inhibitory effect. Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur. Pyruvate kinase from rabbit muscle catalyzes an atp-dependent phosphorylation of glycolate to yield 2-phosphoglycolate. buffered aqueous glycerol solution, 900-1400 units/ml lactic dehydrogenase, 600-1 kda units/ml pyruvate kinase. Applications: Pyruvate kinase from rabbit muscle has been used in a study to assess nuclear magnetic relaxation studies of the conformation of adenosine 5?-triphosphate. it has also been used in a study to investigate heterogeneity of presumably homogeneous protein preparations. Group: Enzymes. Synonyms: Pyruvate Kinase/Lactic Dehydrogenase enzymes; PK/LDH enzymes. PK/LDH enzymes. Activity: 900-1400 units/mL lactic dehydrogenase; 600-1,000 units/mL pyruvate kinase. Stability: -20°C. Form: buffered aqueous glycerol solution. Source: rabbit muscle. Species: Rabbit. Pyruvate Kinase/Lactic Dehydrogenase enzymes; PK/LDH enzymes. Cat No: NATE-0568. | |
| [pyruvate dehydrogenase (acetyl-transferring)] kinase | The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring). Group: Enzymes. Synonyms: PDH kinase; PDHK; PDK; PDK1; PDK2; PDK3; PDK4; pyruvate dehydrogenase kinase; pyruvate dehydrogenase kinase (phosphorylating); pyruvate dehydrogenase kinase activator protein; STK1. Enzyme Commission Number: EC 2.7.11.2. CAS No. 9074-1-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3139; [pyruvate dehydrogenase (acetyl-transferring)] kinase; EC 2.7.11.2; 9074-01-5; PDH kinase; PDHK; PDK; PDK1; PDK2; PDK3; PDK4; pyruvate dehydrogenase kinase; pyruvate dehydrogenase kinase (phosphorylating); pyruvate dehydrogenase kinase activator protein; STK1. Cat No: EXWM-3139. | |
| [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase | A mitochondrial enzyme associated with EC 1.2.4.1 pyruvate dehydrogenase (acetyl-transferring), in the pyruvate dehydrogenase complex. Group: Enzymes. Synonyms: pyruvate dehydrogenase phosphatase; phosphopyruvate dehydrogenase phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase. Enzyme Commission Number: EC 3.1.3.43. CAS No. 9073-70-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3647; [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase; EC 3.1.3.43; 9073-70-5; pyruvate dehydrogenase phosphatase; phosphopyruvate dehydrogenase phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphatase; [pyruvate dehydrogenase (lipoamide)]-phosphate phosphohydrolase. Cat No: EXWM-3647. | |
| 2-oxoglutarate synthase | The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin). Group: Enzymes. Synonyms: 2-ketoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR; 2-oxoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating). Enzyme Commission Number: EC 1.2.7.3. CAS No. 37251-05-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1226; 2-oxoglutarate synthase; EC 1.2.7.3; 37251-05-1; 2-ketoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR; 2-oxoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating). Cat No: EXWM-1226. | |
| 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) | The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, 2-oxobutyrate and 3-methylthiopropanamine. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase. Group: Enzymes. Synonyms: 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chai. Enzyme Commission Number: EC 1.2.7.7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1230; 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin); EC 1.2.7.7; 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase. Cat No: EXWM-1230. | |
| 4-hydroxy-2-oxovalerate aldolase | Requires Mn2+ for maximal activity. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase. Group: Enzymes. Synonyms: 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Enzyme Commission Number: EC 4.1.3.39. CAS No. 37325-52-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4915; 4-hydroxy-2-oxovalerate aldolase; EC 4.1.3.39; 37325-52-3; 4-hydroxy-2-ketovalerate aldolase; HOA; DmpG; 4-hydroxy-2-oxovalerate pyruvate-lyase; 4-hydroxy-2-oxopentanoate pyruvate-lyase; BphI; 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming). Cat No: EXWM-4915. | |
| 4-phosphoerythronate dehydrogenase | This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid. cf. EC 1.1.1.399, 2-oxoglutarate reductase. Group: Enzymes. Synonyms: PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase. Enzyme Commission Number: EC 1.1.1.290. CAS No. 125858-75-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0199; 4-phosphoerythronate dehydrogenase; EC 1.1.1.290; 125858-75-5; PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase. Cat No: EXWM-0199. | |
| [acetyl-CoA carboxylase]-phosphatase | Simultaneously dephosphorylates and activates EC 6.4.1.2 acetyl-CoA carboxylase. Acts similarly on EC 1.1.1.88 (hydroxymethylglutaryl-CoA reductase), EC 2.4.1.1 (phosphorylase), EC 2.4.1.11 [glycogen(starch) synthase], and dephosphorylates phosphoprotamine and 4-nitrophenyl phosphate. Not identical to EC 3.1.3.17 ([phosphorylase] phosphatase ) or EC 3.1.3.43 {[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase}. Group: Enzymes. Enzyme Commission Number: EC 3.1.3.44. CAS No. 77000-10-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3648; [acetyl-CoA carboxylase]-phosphatase; EC 3.1.3.44; 77000-10-3. Cat No: EXWM-3648. | |
| Adaptaquin | Adaptaquin is an inhibitor of hypoxia-inducible factor (HIF) prolyl hydroxylase 2 (PHD2) with IC50 value of 2 μM in a reporter assay using SH-SY5Y-ODD-Luc cells. It displays neuroprotective effects and enhances functional recovery in rodent intracerebral hemorrhage models by inhibition of ATF4 dependent genes. It reduces neuronal death and behavioral deficits after intracerebral hemorrhage (ICH) in several rodent models. It blocks glutamate induced ROS production in HT-22 cells, independent of MnSOD. It stabilizes HIF-1α protein and induces expression of the HIF1-regulated genes EPO and VEGF in SH-SY5Y human neuroblastoma cells. It is used in ischemic injury research, renal anemia, and used as an antioxidant. It is also used in pyruvate dehydrogenase (PDH) related research. Synonyms: 7-[(4-Chlorophenyl)[(3-hydroxy-2-pyridinyl)amino]methyl]-8-quinolinol. Grades: ≥97% by HPLC. CAS No. 385786-48-1. Molecular formula: C21H16ClN3O2. Mole weight: 377.82. |  |
| Alanine dehydrogenase, expressed in E. coli | Alanine dehydrogenase, expressed in E. coli is a microbial enzyme that catalyzes a reversible conversion of L-alanine to pyruvate [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9029-6-5. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P2854. |  |
| Alanine Dehydrogenase from Bacillus cereus, Recombinant | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-cysteine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alan. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: > 350 units/ml. Storage: -20°C. Source: E. coli. Species: Bacillus cereus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0044. | |
| α-Lipoic Acid | α-Lipoic Acid is a metabolic antioxidant that regulates NFκB signal transduction and can protect against oxidative injury. The exogenous compound is reduced intracellularly by enzymes. Its reduced form is involved in radical scavenging, recycling of other antioxidants, accelerating GSH synthesis, and regulating transcription factor activity, specifically NFkappaB. It also acts as a conenzyme that is required for the activity of pyruvate dehydrogenase and glycine decarboxylase, among other enzyme complexes. Studies show that it can prevent a decrease in the renal antioxidant defense system and prevent the increase of lipid peroxidation, platinum content and plasma creatinine concentrations. In other studies, lipoic acid decreased the phagocytosis of myelin by macrophages, acting as a non-specific scavenger of reactive oxygen species (ROS). Applications: A metabolic antioxidant that regulates nf-κb signal transduction. Group: Coenzymes. Synonyms: DL-Thioctic Acid; DL-6,8-Dithiooctanoic acid; 1,2-Dithiolane-3-valeric acid. CAS No. 1077-28-7. Purity: ≥95%. Mole weight: 206.32. Form: Solid. DL-Thioctic Acid; DL-6,8-Dithiooctanoic acid; 1,2-Dithiolane-3-valeric acid; α-Lipoic Acid; 1077-28-7. Cat No: COEC-041. | |
| Chemically modified Porcine L-Lactate Dehydrogenase | Dehydrogenase that catalyzes the interconversion of L(+)-lactate to pyruvate. Take advantage of the enhanced liquid stability of this enzyme. Rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase (l-ldh), chemically modified, in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase, aldolase, aminotransferases, glutamate dehydrogenase). Group: Enzymes. Synonyms: lactic acid dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; L-lactate dehydrogenase; L-LDH; LAD; LD; Lactate. LDH. Activity: >25 U/mg lyophilizate; >150 U/mg protein. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White lyophilizate. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: DIA-279. | |
| D-2-hydroxyacid dehydrogenase (NAD+) | The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+). Group: Enzymes. Synonyms: LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous). Enzyme Commission Number: EC 1.1.1.345. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0260; D-2-hydroxyacid dehydrogenase (NAD+); EC 1.1.1.345; LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous). Cat No: EXWM-0260. | |
| DCA | DCA is a mitochondrial pyruvate dehydrogenase kinase (PDK) inhibitor that shifts pyruvate metabolism from glycolysis and lactate production to glucose oxidation in the mitochondria. DCA also induces apoptosis and reverses the KV1.5 channels downregulation in cancer. Synonyms: Sodium dichloroacetate; Sodium 2,2-dichloroacetate; Dichloroacetic acid sodium salt. CAS No. 2156-56-1. Molecular formula: C2HCl2NaO2. Mole weight: 150.92. | |
| Diaphorase 22 from Recombinant E.coli | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoami...(NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Mole weight: ca. 110,000. Activity: >150 U/mg protein. Storage: Store at -20°C. Form: Lyophilized. Source: E. coli. LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate d | |
| dihydrolipoyl dehydrogenase | A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or...tase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1648; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; LDP-Glc; LDP-Val; dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxido | |
| dihydrolipoyllysine-residue acetyltransferase | A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalysed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A. Group: Enzymes. Synonyms: acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; d. Enzyme Commission Number: EC 2.3.1.12. CAS No. 9032-29-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2058; dihydrolipoyllysine-residue acetyltransferase; EC 2.3.1.12; 9032-29-5; acetyl-CoA:dihydrolipoamide S-acetyltransferase; dihydrolipoamide S-acetyltransferase; dihydrolipoate acetyltransferase; dihydrolipoic transacetylase; dihydrolipoyl acetyltransferase; lipoate acetyltransferase; lipoate transacetylase; lipoic acetyltransferase; lipoic acid acetyltransferase; lipoic transacetylase; lipoylacetyltransferase; thioltransacetylase A; transacetylase X; enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase; acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase. Cat No: EXWM-2058. | |
| D-Lactate dehydrogenase from Bacteria, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Mole weight: 44 kD (SDS-PAGE). Activity: > 800 U/mg Protein. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-1042. | |
| D-lactate Dehydrogenase from E. coli, Recombinant | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This protein is fused with 6x his tag at n terminus and the protein has a calculated mw of 39.1 kda (353aa). Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c . Enzyme Commission Number: EC 1.1.1.28. Purity: > 95% by SDS-PAGE. D-LDH. Mole weight: 39.1 kDa. Activity: > 200 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D- (-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D- (-)-lactic cytochrome c reductase; D-lactate Dehydrogenase. Cat No: NATE-1654. | |
| D-Lactate dehydrogenase, Microorganism | D-Lactate dehydrogenase, Microorganism (D-LDH) is an oxidoreductase that uses NAD + or NADP + as an acceptor and acts on the donor CH-OH group, and can catalyze the oxidation of D-lactate to pyruvate. D-Lactate dehydrogenase widely exists in bacteria and fungi, and is often used in biochemical research [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: D-LDH. CAS No. 9028-36-8. Pack Sizes: 500 U; 1 KU. Product ID: HY-P2897. | |
| D-lysopine dehydrogenase | In the reverse reaction, a number of L-amino acids can act instead of L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate can act instead of pyruvate. Group: Enzymes. Synonyms: D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase; 2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Enzyme Commission Number: EC 1.5.1.16. CAS No. 65187-41-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1497; D-lysopine dehydrogenase; EC 1.5.1.16; 65187-41-9; D-lysopine synthase; lysopine dehydrogenase; D(+)-lysopine dehydrogenase; 2-N-(D-1-carboxyethyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming). Cat No: EXWM-1497. | |
| Galloflavin | Galloflavin is a potent lactate dehydrogenase (LDH) inhibitor. The calculated K i s for pyruvate are 5.46 μM (LDH-A) and 15.06 μM (LDH-B). Galloflavin hinders the proliferation of cancer cells by blocking glycolysis and ATP production [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 568-80-9. Pack Sizes: 10 mM * 1 mL; 1 mg; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-W040118. | |
| Galloflavin Potassium salt | Galloflavin Potassium salt is an inhibitor of human lactate dehydrogenase (LDH) (Ki = 5.46 and 15.1 μM for LDH-A and LDH-B, respectively, in competition with pyruvate) with anticancer activity. Galloflavin inhibits lactate production and decreases ATP synthesis in PLD/PRF/5 cells. Synonyms: NSC-107022 potassium; NSC 107022 potassium; NSC107022 potassium; 3,8,9,10-Tetrahydroxypyrano[3,2-c][2]benzopyran-2,6-dione potassium salt. Grades: ≥95% by HPLC. CAS No. 1780260-20-9. Molecular formula: C12H5O8K. Mole weight: 316.26. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| Glycerokinase from Cellulomonas sp. | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. Phosphoryl moiety of atp to one of the primary hydroxyl group of glycerol, forming sn-glycerol-3-p. the enzyme has the highest specificity for glycerol, and also phosphorylates dihydroxyacetone and glyceraldehyde (table 1,2). mg++ is essentially required for the reaction. Applications: This enzyme is useful for enzymatic deter...se, g3o-301, g3o-311, g3o-321) or pyruvate kinase (pyk-301) and lactate dehydrogenase (lcd-209, lcd-211), lipoprotein lipase (lpl-311, lpl-314) in clinical analysis. Group: Enzymes. Synonyms: EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. Activity: 20 U/mg-solid or more. Storage: -20°C. Form: Lyophilized powder containing phosphate buffer salts and sodium gluconate. Source: Cellulomonas sp. EC 2.7.1.30; glycerokinase; GK; ATP:glycerol-3-phosphotransferase; glycerol kinase (phosphorylating); glyceric kinase; 9030-66-4. Cat No: NATE-0287. | |
| Glycerokinase from Microorganism | Glycerol kinase is a phosphotransferase enzyme involved in triglycerides and glycerophospholipids synthesis. Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate. Applications: This enzyme is useful for enzymatic determination of glycerol and triglyceride when coupled with glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate oxidase or pyruvate kinase and lactate dehydrogenase, lipoprotein lipase in clinical analysis. Group: Enzymes. Synonyms: glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. Activity: 30 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Cat No: DIA-149. | |
| Hydroxypyruvic acid | Hydroxypyruvic acid (β-Hydroxypyruvic acid) is an intermediate in the metabolism of glycine, serine and threonine. Hydroxypyruvic acid is a substrate for serine-pyruvate aminotransferase and glyoxylate reductase/hydroxypyruvate reductase. Hydroxypyruvic acid is involved in the metabolic disorder which is the dimethylglycine dehydrogenase deficiency pathway. Uses: Scientific research. Group: Natural products. Alternative Names: β-Hydroxypyruvic acid; 3-Hydroxypyruvic acid. CAS No. 1113-60-6. Pack Sizes: 1 mg; 5 mg. Product ID: HY-113013. | |
| indolepyruvate ferredoxin oxidoreductase | Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin). Group: Enzymes. Synonyms: 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR. Enzyme Commission Number: EC 1.2.7.8. CAS No. 158886-06-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1231; indolepyruvate ferredoxin oxidoreductase; EC 1.2.7.8; 158886-06-7; 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR. Cat No: EXWM-1231. | |
| JX 06 | JX 06 is a potent, selective and covalent pyruvate dehydrogenase kinase (PDK) 1/2/3 inhibitor with IC50 values of 49, 101 and 313 nM for PDK1, PDK2 and PDK3, respectively. It suppresses A549 lung cancer cell proliferation in vitro and reduces tumor volume of A549 xenografts in mice. Synonyms: JX-06; JX06; Bis(morpholinothiocarbonyl) Disulfide; 4, 4'- (Dithiodicarbonothioyl) bis[morpholine]; 4-Morpholinethiocarbonyl Disulfide; Dimorpholinethiuram Disulfide; Disulfide, bis(4-Morpholinylthioxomethyl); NSC 402538; bis(Oxydi-2,1-ethanediyl)-thiuram Disulfide. Grades: ≥98% by HPLC. CAS No. 729-46-4. Molecular formula: C10H16N2O2S4. Mole weight: 324.51. | |
| JX-06 | JX-06 is a potent and selective pyruvate dehydrogenase kinase (PDK) 1/2/3 inhibitor (IC50 values are 28, 49 and 313 nM for PDK2, PDK1 and PDK3, respectively). JX06 Selectively Inhibits Pyruvate Dehydrogenase Kinase PDK1 by a Covalent Cysteine Modification. JX06, as a selective covalent inhibitor of PDK1 in cells, forms a disulfide bond with the thiol group of a conserved cysteine residue (C240) based on recognition of a hydrophobic pocket adjacent to the ATP pocket of the PDK1 enzyme. Group: Inhibitors. Alternative Names: JX-06; JX 06; JX06. CAS No. 729-46-4. Molecular formula: C10H16N2O2S4. Mole weight: 324.49. Appearance: Solid powder. Purity: >98%. IUPACName: Bis(morpholinothiocarbonyl) disulfide. Canonical SMILES: S=C(SSC(N1CCOCC1)=S)N2CCOCC2. Catalog: ACM729464. |  |
| lactaldehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-lactaldehyde:NAD+ oxidoreductase. Other names in common use include L-lactaldehyde:NAD+ oxidoreductase, and nicotinamide adenine dinucleotide (NAD+)-linked dehydrogenase. This enzyme participates in pyruvate metabolism. Group: Enzymes. Synonyms: L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase. Enzyme Commission Number: EC 1.2.1.22. CAS No. 37250-90-1. Lactaldehyde dehydrogenase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1128; lactaldehyde dehydrogenase; EC 1.2.1.22; 37250-90-1; L-lactaldehyde:NAD oxidoreductase; nicotinamide adenine dinucleotide (NAD)-linked dehydrogenase. Cat No: EXWM-1128. | |
| Lactate Dehydrogenase from Chicken Heart, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Purity: > 96% (SDS-PAGE). LDH. Activity: >90%. (>200U/mL). Storage: -20°C. Form: Lyophilized. Source: E. coli. Species: Chicken Heart. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0383. | |
| Lactic Dehydrogenase, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Source: E. coli. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Cat No: NATE-0381. | |
| Leelamine | Leelamine, a diterpene molecule, has weak affinity for the human central cannabinoid (CB1) and peripheral cannabinoid (CB2) receptors. Leelamine is also a PDK(pyruvate dehydrogenase kinase inhibitor). Synonyms: [(1R,4aS,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,9,10,10a-hexahydrophenanthren-1-yl]methanamine; dehydroabietylamine; DEHYDROABIETYLAMINE; (+)-Dehydroabietylamine; Dehydroabiethylamine; 16496-99-4 Leelamine (hydrochloride). Grades: ≥90%. CAS No. 1446-61-3. Molecular formula: C20H31N. Mole weight: 285.5. | |
| Leelamine | Leelamine is an orally active pyruvate dehydrogenase kinase ( PDK ) inhibitor with an IC 50 value of 9.5 μM, showing a blood glucose lowering effect in the diabetic mouse. Leelamine is also a weak agonist of cannabinoid receptors CB1 and CB2. Leelamine decreases mitotic activity, prostate-specific antigen expression and induces Apoptosis to cell death in cancer cells [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. CAS No. 1446-61-3. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g. Product ID: HY-W005629. | |
| Leelamine hydrochloride | Leelamine is a diterpene amine exhibiting low affinity for the human central cannabinoid (CB1) and peripheral cannabinoid (CB2) receptors. It also acts as an inhibitor of pyruvate dehydrogenase kinase (PDK). Leelamine inhibits intracellular cholesterol transport and suppresses cancer cell growth. Synonyms: Lylamine hydrochloride; Dehydroabiethylamine hydrochloride; [(1R,4aS,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,9,10,10a-hexahydrophenanthren-1-yl]methanamine hydrochloride. Grades: ≥98%. CAS No. 16496-99-4. Molecular formula: C20H31N·HCl. Mole weight: 321.9. | |
| lipoate-protein ligase | Requires Mg2+. This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid. The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). Lipoylation is essential for the function of these enzymes. The enzyme can also use octanoate instead of lipoate. Group: Enzymes. Synonyms: lplA (gene name); lplJ (gene name); lipoate protein ligase; lipoate-protein ligase A; LPL; LPL-B. Enzyme Commission Number: EC 6.3.1.20. CAS No. 144114-18-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5723; lipoate-protein ligase; EC 6.3.1.20; 144114-18-1; lplA (gene name); lplJ (gene name); lipoate protein ligase; lipoate-protein ligase A; LPL; LPL-B. Cat No: EXWM-5723. | |
| lipoyl amidotransferase | In the bacterium Listeria monocytogenes the enzyme takes part in a pathway for scavenging of lipoic acid. The enzyme is bound to 2-oxo-acid dehydrogenases such as the pyruvate dehydrogenase complex, where it transfers the lipoyl moiety from lipoyl-[glycine cleavage system H] to the E2 subunits of the complexes. Group: Enzymes. Synonyms: LipL (gene name, ambiguous). Enzyme Commission Number: EC 2.3.1.200. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2145; lipoyl amidotransferase; EC 2.3.1.200; LipL (gene name, ambiguous). Cat No: EXWM-2145. | |
| lipoyl(octanoyl) transferase | This is the first committed step in the biosynthesis of lipoyl cofactor. Lipoylation is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. Examples of such lipoylated proteins include pyruvate dehydrogenase (E2 domain), 2-oxoglutarate dehydrogenase (E2 domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate. The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8, lipoyl synthase. An alternative lipoylation pathway invol...rase; octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase. Enzyme Commission Number: EC 2.3.1.181. CAS No. 392687-64-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2123; lipoyl(octanoyl) transferase; EC 2.3.1.181; 392687-64-8; LipB; lipoyl (octanoyl)-[acyl-carrier-protein]-protein N-lipoyltransferase; lipoyl (octanoyl)-acyl carrier protein:protein transferase; lipoate/octanoate transferase; lipoyltransferase; octanoyl-[acyl carrier protein]-protein N-octanoyltransferase; lipoyl(octanoyl)transferase; octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase. Cat No: EXWM-2123. | |
| L-Lactate Dehydrogenase from Porcine, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: High purity l-lactate dehydrogenase (porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: ~ 330 U/mg. Storage: > 2 years at 4°C. Form: In 3.2 M ammonium sulphate. Source: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-1105. | |
| L-Lactate dehydrogenase, Microorganism | L-Lactate dehydrogenase, Microorganism (LAD) is a redox enzyme. L-Lactate dehydrogenase catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: LAD. CAS No. 9001-60-9. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-P2807. | |
| L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Recombinant, expressed in e. coli, lyophilized powder, > 200 units/mg protein (lowry). Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 200 units/mg protein (Lowry). Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Bacillus stearothermophilus. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0382. | |
| Malate dehydrogenase from Bacteria, Recombinant | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mit...EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Mole weight: 40 kD (SDS-PAGE). Activity: > 550 units / mg. Storage: Below -20°C. Form: Lyophilized powder. Source: E. coli. Species: Bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Cat No: NATE-1038. | |
| Native Bacillus stearothermophilus Alanine Dehydrogenase | L-Alanine dehydrogenase is a stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the generation of pyruvate during sporulation. Applications: The enzyme is useful for determination of l-alanine. Group: Enzymes. Synonyms: L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Mole weight: ca. 230,000; Subunit molecular weight : ca. 38,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Bacillus stearothermophilus. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-1899. | |
| Native Bacillus subtilis L-Alanine Dehydrogenase | L-Alanine dehydrogenase is an A-stereospecific dehydrogenase that catalyzes the reversible deamination of L-alanine to pyruvate and ammonium. It is important for the geneRation of pyruvate during sporulation. L-Alanine dehydrogenase from Bacillus subtilis has a predominately ordered kinetic mechanism in which NAD binds before L-alanine. Subsequently, ammonia, pyruvate, and NADH are released in that specific order. Optimal pH for the amination reaction is 8.8-9.0, whereas it is 10-10.5 for the deamination reaction. The enzyme is inactivated by divalent metal ions and p-chloromercuribenzoate, mercuric ion being most effective. The inactivation may be reversed by L-or D-...genase. Enzyme Commission Number: EC 1.4.1.1. CAS No. 9029-6-5. AlaDH. Activity: Type I, ~30 units/mg protein (Lowry); Type II, > 20 units/mg protein (Lowry). Storage: -20°C. Form: Type I, buffered aqueous glycerol solution, Solution in 50% glycerol containing 10 mM potassium phosphate buffer, pH 7.7; Type II, ammonium sulfate suspension, Suspension in 2.4 M (NH4)2SO4 solution, pH 7.0. Source: Bacillus subtilis. L-Alanine Dehydrogenase; Alanine dehydrogenase; EC 1.4.1.1; 9029-06-5; AlaDH; NAD+-linked alanine dehydrogenase; alpha-alanine dehydrogenase; NAD+-dependent alanine dehydrogenase; alanine oxidoreductase; NADH-dependent alanine dehydrogenase. Cat No: NATE-0043. | |
| Native Bovine L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: For use in enzymatic determination of lactate or pyruvate. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nL. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5. Source: Bovine heart. Species: Bovine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0409. | |
| Native Chicken L-Lactic Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 1.3 M (NH4)2SO4, pH 6.0. Source: Chicken heart. Species: Chicken. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0411. | |
| Native Human Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0380. | |
| Native Human Lactate Dehydrogenase 1 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0384. | |
| Native Human Lactate Dehydrogenase 2 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0386. | |
| Native Human Lactate Dehydrogenase 3 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0388. | |
| Native Human Lactate Dehydrogenase 4 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; validation studies; manufacturing. Group: Enzymes. Synonyms: LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 35 U/mg protein (> 110 U/mL). Stability: 2 years. Storage: 2-8°C. Form: Liquid; Suspension in 3.1 M ammonium sulfate, 20 mM tris chloride, 1 mM DTT, 1 mM EDTA, pH 7.5. Source: Human Liver. Species: Human. LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme; Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0965. | |
| Native Human Lactate Dehydrogenase 5 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Liver. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0390. | |
| Native Lactate Dehydrogenase from Thermophillic bacteria | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic test and biosensors; nadh recycling. this enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-400. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade I | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. benefit from the...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >180 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0976. | |
| Native Lactobacillus delbrückii D-Lactate Dehydrogenase, Grade II | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Dehydrogenase that catalyzes the interconversion of d(-)-lactate to pyruvate. rely on the proven diagnostic quality of this product. Applications: U...ase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. CAS No. 9028-36-8. D-LDH. Activity: >150 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White to yellowish lyophilizate. Source: Lactobacillus delbrückii. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0977. | |
| Native Lactobacillus leichmanii D-Lactic Dehydrogenase | D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: In the food industry, the primary catalysis is coupled to conversion of nadh and h+ to nad+ with diaphorase coupled with converting the non-fluorescent resazurin to the highly fluorescent substance resorufin to measure the content of d-lactate in food products. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 30 units/mg protein; ~1000 U/mL; 250-500 units/mg protein (biuret); 150-300 units/mg protein; 1,000-3,000 units/mg protein (biuret). Storage: 2-8°C. Form: Suspension in 3.2 M (NH4)2SO4, 0.1 M potassium phosphate, pH 7.0. Source: Lactobacillus leichmanii. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0195. | |
| Native Leuconostoc mesenteroides D-Lactic Dehydrogenase | In enzymology, a D-lactate dehydrogenase is an enzyme that catalyzes the chemical reaction: (D)-lactate + 2 ferricytochrome c<-> pyruvate + 2 ferrocytochrome c. Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. Group: Enzymes. Synonyms: EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: 1,000-3,000 units/mg protein (biuret). Stability: 2-8°C. Form: ammonium sulfate suspension. Source: Leuconostoc mesenteroides. EC 1.1.1.28; D-Lactic Dehydrogenase; 9028-36-8; (D)-lactate:ferricytochrome-c 2-oxidoreductase; lactic acid dehydrogenase; D-lactate (cytochrome) dehydrogenase; cytochrome-dependent D-(-)-lactate dehydrogenase; D-lactate-cytochrome c reductase; D-(-)-lactic cytochrome c reductase. Cat No: NATE-0196. | |
| Native Malate dehydrogenase (Decarboxylating) from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses ...; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.38; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.38. CAS No. 9080-52-8. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD- | |
| Native Malate dehydrogenase from Thermophillic bacteria | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner...e dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidored | |
| Native Microorganism D-lactate dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: 400U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Storage: Store at -20°C. Form: Freeze dried powder. Source: Microorganism. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-207. | |
| Native Microorganism Glycerol Kinase | The activity of glycerol kinase is found widely in nature. In microorganisms GK makes possible the utilization of glycerol as a carbon source. In mammals the enzyme represents a juncture of sugar and fat metabolism; The enzyme is important to the clinical chemist in the determination of glycerol. GK is also useful in the assay of glyceraldehydes and dihydroxyacetone following their quantitative reduction to glycerol with sodium borohydride. Applications: This enzyme is useful for enzymatic determination of glycerol and triglyceride when coupled with glycerol-3-phosphate dehydrogenase, glycerol-3-phosphate oxidase or pyruvate kinase and lactate dehydrogenase, lipoprotein lipase in clinical analysis. Group: Enzymes. Synonyms: glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Enzyme Commission Number: EC 2.7.1.30. CAS No. 9030-66-4. GK. Mole weight: approx. 220 kDa (by gel filtration). Activity: Grade? 30 U/mg-solid or more. Stability: Stable at-20°C. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Cat No: DIA-149. | |
| Native Microorganism Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitoch...-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. Activity: 40U/mg-solid or more. Appearance: Slightly yellowish amorphous powder, lyophilized. Storage: Stable at-20°C for at least one year. Form: Freeze dried powder. Source: Microorganism. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific m | |
| Native Porcine heart Lactate dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 115 kDa±6,500. Activity: Grade? 2,000U/ml or more. Stability: Stable at 5°C for at least one year. Appearance: Crystalline suspension in 1.6M ammonium sulfate solution. Source: Porcine heart. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-206. | |
| Native Porcine Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: ~136,700. Activity: > 100 U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Lyophilized. Source: Porcine Muscle. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0964. | |
| Native Porcine L-Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Dehydrogenase that catalyzes the interconversion of specific for l(+)-lactate to pyruvate. apply this ready-to-use enzyme directly in your diagnostic test. rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase,...ehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. CAS No. 9001-60-9. LDH. Activity: >550 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5. Source: Porcine muscle. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0982. | |
Our database is helping our users find suppliers everyday.
