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Aluminium+oxide+acidic
Catalog Number:
(10395-514)
Supplier:
Bioss
Description:
Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. Malate dehydrogenase 1 (MDH1) is localized to the cytoplasm and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria.
Catalog Number:
(10395-516)
Supplier:
Bioss
Description:
Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. Malate dehydrogenase 1 (MDH1) is localized to the cytoplasm and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria.
Supplier:
ALADDIN SCIENTIFIC
Description:
Reactant for: 1.Preparation of (aryl)oxadiazolobenzoxazinones via Suzuki-Miyaura reaction. 2.Copper-catalyzed oxidative amination of benzoxazoles and related azoles via C-H and C-N bond activation. 3.Synthesis of N-(alkoxyphenyl)-aminocarbonylbenzoic acid derivatives as protein tyrosine phophatase 1B inhibitors. 4. Preparation of lipophilic deoxy-xylulose-phosphate reductoisomerase inhibitors. 5.Synthesis of benzoxazole benzenesulfonamides as allosteric inhibitors of fructose-1,6-bisphosphatase.application:Reactant for:Preparation of (aryl)oxadiazolobenzoxazinones via Suzuki-Miyaura reactionCopper-catalyzed oxidative amination of benzoxazoles and related azoles via C-H and C-N bond activationSynthesis of N-(alkoxyphenyl)-aminocarbonylbenzoic acid derivatives as protein tyrosine phophatase 1B inhibitorsPreparation of lipophilic deoxy-xylulose-phosphate reductoisomerase inhibitorsSynthesis of benzoxazole benzenesulfonamides as allosteric inhibitors of fructose-1,6-bisphosphatase
Catalog Number:
(10388-430)
Supplier:
Bioss
Description:
Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.
Catalog Number:
(76107-956)
Supplier:
Bioss
Description:
The Isocitrate dehydrogenase cytoplasmic enzyme is a homodimer of 416 residues that belongs to the isocitrate and isopropylmalate dehydrogenases family. IDHC catalyzes the third step of the citric acid cycle, which involves the oxidative decarboxylation of isocitrate, forming ketoglutarate and CO₂ in a two step reaction. The first step involves the oxidation of isocitrate to the intermediate oxalosuccinate, while the second step involves the production of ketoglutarate. During this process, either NADH or NADPH is produced along with CO₂. Ca²⁺ can bind to IDHC as a complex with isocitrate, acting as a competitive inhibitor of Mg²⁺. The IDHC enzyme is inactivated by phosphorylation at Ser-113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock. IDHC is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle.
Catalog Number:
(80108-488)
Supplier:
MilliporeSigma
Description:
Aldehyde dehydrogenase from yeast catalyzes the oxidation of acetaldehyde to acetic acid.
Catalog Number:
(10427-830)
Supplier:
Bioss
Description:
AARE (Acylamino-acid-releasing enzyme) is also known as Acyl-peptide hydrolase. It catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus corresponding to the protein are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma.
Supplier:
Thermo Scientific Chemicals
Description:
Carbonylation, oxidation and C-C bond formation
Catalog Number:
(80602-310)
Supplier:
MilliporeSigma
Description:
Recombinant, <i>Aspergillus niger</i> glucose oxidase catalyzes the oxidation of β-D-glucose to D-glucono-ω-lactone and hydrogen peroxide and also catalyzes the conversion of D-glucono-ω-lactone to gluconic acid. Used for enzymatic assay of glucose concentration.
Supplier:
BeanTown Chemical
Description:
CAS: 10213-10-2; EC No: 236-743-4; MDL No: MFCD00149190; RTECS: YO7900000
Crystalline; Linear Formula: Na2WO4·2H2O ; MW: 329.86
Melting Point: 698°
Density (g/mL): 4.18
Catalog Number:
(10395-646)
Supplier:
Bioss
Description:
Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2.
Catalog Number:
(10390-272)
Supplier:
Bioss
Description:
Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).
Catalog Number:
(10320-938)
Supplier:
Bioss
Description:
Oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized.
Catalog Number:
(10110-072)
Supplier:
Prosci
Description:
Malate dehydrogenase 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 may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria.Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. The protein encoded by this gene is localized to the mitochondria and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Catalog Number:
(PI22106)
Supplier:
Invitrogen
Description:
Thermo Scientific Pierce EMCH is a mid-length, maleimide-and-hydrazide crosslinker for conjugating sulfhydryls (cysteines) to carbonyls (aldehyde or ketones, such as those formed by oxidation of glycoprotein carbohydrates).
Catalog Number:
(10100-300)
Supplier:
Prosci
Description:
ACSBG2 belongs to the ATP-dependent AMP-binding enzyme family, bubblegum subfamily.ACSBG2 mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. It is able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. ACSBG2 has increased ability to activate oleic and linoleic acid. It may play a role in spermatogenesis.
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