2. Metabolic Disease

Metabolic Disease

Metabolic Disease

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Metabolic diseases is defined by a constellation of interconnected physiological, biochemical, clinical, and metabolic factors that directly increases the risk of cardiovascular disease, type 2 diabetes mellitus, and all cause mortality. Associated conditions include hyperuricemia, fatty liver (especially in concurrent obesity) progressing to nonalcoholic fatty liver disease, polycystic ovarian syndrome (in women), erectile dysfunction (in men), and acanthosis nigricans. Metabolic disease modeling is an essential component of biomedical research and a mandatory prerequisite for the treatment of human disease. Somatic genome editing using CRISPR/Cas9 might be used to establish novel metabolic disease models.

Cat. No. Product Name CAS No. Purity Chemical Structure
  • HY-P2726A
    Aldolase, Spinach 98%
    Aldolase, Spinach (EC 4.1.2.13) is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase, Spinach (EC 4.1.2.13) can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate.
    Aldolase, Spinach
  • HY-P2733A
    Glycerol 3-phosphate Oxidase, Pedio coccus sp. 9046-28-0 98%
    Glycerol-3-phosphate oxidase, Pedio coccus sp. (GPO, Pedio coccus sp.) is a key intermediate in glycerol metabolism. Glycerol-3-phosphate oxidase is the skeleton of phospholipids in membrane lipids, and also a substrate in the respiratory chain. Glycerol-3-phosphate oxidase produces electrons through oxidation.
    Glycerol 3-phosphate Oxidase, Pedio coccus sp.
  • HY-P2733B
    Glycerol 3-phosphate Oxidase, Aerococcus viridans 9046-28-0
    Glycerol-3-phosphate oxidase, Aerococcus viridans (GPO, Aerococcus viridans) is a key intermediate in glycerol metabolism. Glycerol-3-phosphate oxidase is the skeleton of phospholipids in membrane lipids, and also a substrate of respiratory chain. Glycerol-3-phosphate oxidase produces electrons through oxidation.
    Glycerol 3-phosphate Oxidase, Aerococcus viridans
  • HY-P2733D
    Glycerol 3-phosphate Oxidase, Streptococcus thermophilus
    Glycerol 3-phosphate Oxidase, Streptococcus thermophilus (EC 1.1.3.21), is an oxidoreductase that acts on the CH-OH group in donor molecules and uses oxygen as an acceptor. Glycerol 3-phosphate Oxidase participates in glycerophospholipid metabolism and utilizes a cofactor, FAD. The two substrates of Glycerol 3-phosphate Oxidase are sn-glycerol-3-phosphate and O2, while its two products are glycerophosphate and H2O2.
    Glycerol 3-phosphate Oxidase, Streptococcus thermophilus
  • HY-P2739A
    Citrate Synthase, Porcine
    Citrate Synthase, Porcine (EC 4.1.3.7), catalyzes the conversion of citrate to acetyl-CoA in the presence of coenzyme A, releasing water and oxaloacetate. Citrate Synthase can be inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citrate-CoA.
    Citrate Synthase, Porcine
  • HY-P2739B
    Citrate Synthase, Pigeon
    Citrate Synthase, Pigeon (EC 4.1.3.7) catalyses the conversion of Citrate to acetyl-CoA in the presence of coenzyme-A with the release of H2O and oxaloacetate. Citrate Synthase, Pigeon (EC 4.1.3.7) is inhibited by fluoroacetyl-CoA, palmitoyl-CoA, and citroyl-CoA.
    Citrate Synthase, Pigeon
  • HY-P2740B
    Alcohol dehydrogenase, yeast 9031-72-5 98%
    Alcohol dehydrogenase, yeast is an alcohol dehydrogenase expressed in yeast. It can catalyze the conversion between ethanol and acetaldehyde, while also reducing NAD or NADP, and it plays a role in glycolysis and aerobic respiration.
    Alcohol dehydrogenase, yeast
  • HY-P2740C
    Alcohol Dehydrogenase(NADP+ dependent), Thermoanaerobium brockii
    Alcohol Dehydrogenase(NADP+ dependent), Thermoanaerobium brockii (EC 1.1.1.2) is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue.
    Alcohol Dehydrogenase(NADP+ dependent), Thermoanaerobium brockii
  • HY-P2741A
    Maltose phosphorylase, Bacteria
    Maltose phosphorylase, Bacteria (EC 2.4.1.8) is a dimeric enzyme that catalyzes maltose and inorganic phosphate into β-D-glucose-1-phosphate and glucose.
    Maltose phosphorylase, Bacteria
  • HY-P2742A
    L-Ascorbate oxidase, Cucumber 9029-44-1 98%
    L-Ascorbate oxidase, Cucumber belongs to the family of oxidoreductases acting on diphenols and related substances as donor with oxygen as acceptor. L-Ascorbate oxidase, Cucumber catalyses the oxidation of L‐Ascorbate (HY-B0166) with oxygen to dehydroascorbate with the generation of water. L-Ascorbate oxidase, Cucumber can be used in baking processes and cereal‐based processes.
    L-Ascorbate oxidase, Cucumber
  • HY-P2742B
    Ascorbate oxidase, acremonium sp 9029-44-1 98%
    Ascorbate oxidase, acremonium sp is a member of the multicopper blue oxidase family and primarily exists in plants as a free enzyme in the cytoplasm or bound to the cell wall. Ascorbate oxidase, acremonium sp has a high activity in catalyzing the oxidation of ascorbic acid to dehydroascorbic acid, regulating various cellular processes related to plant growth, protection, and development. Ascorbate oxidase, acremonium sp can be used to detect hydrogen peroxide.
    Ascorbate oxidase, acremonium sp
  • HY-P2742C
    Ascorbate Oxidase, Zucchini
    Ascorbate Oxidase, Zucchini (EC 1.10.3.3), belongs to the oxidoreductase family, using diphenols and related substances as donors and oxygen as acceptors. Ascorbate Oxidase participates in ascorbic acid metabolism. Ascorbate Oxidase uses a cofactor-copper. Its two substrates are L-ascorbic acid and O2, while its two products are dehydroascorbic acid and H2O.
    Ascorbate Oxidase, Zucchini
  • HY-P2743A
    Choline Oxidase, Alcaligenes sp.
    Choline oxidase, Alcaligenes sp. (EC 1.1.3.17) is an oxidoreductase that acts on the CH-OH group in a donor molecule and uses oxygen as an acceptor. The two substrates of Choline oxidase, Alcaligenes sp. (EC 1.1.3.17) are choline and O2, and the two products are betaine aldehyde and H2O2.
    Choline Oxidase, Alcaligenes sp.
  • HY-P2743B
    Choline oxidase, Arthrobacter globiformis
    Choline oxidase, Arthrobacter globiformis (EC 1.1.3.17) is an oxidoreductase that acts on the CH-OH group in a donor molecule and uses oxygen as an acceptor. The two substrates of Choline oxidase, Arthrobacter globiformis (EC 1.1.3.17) are choline and O2, and the two products are betaine aldehyde and H2O2.
    Choline oxidase, Arthrobacter globiformis
  • HY-P2749A
    L-Glutamine Synthetase, Escherichia coli
    L-Glutamine Synthetase, Escherichia coli (EC 6.3.1.2) is an enzyme that plays an important role in nitrogen metabolism, catalyzing the condensation of glutamate and ammonia to produce glutamine. L-Glutamine Synthetase, Escherichia coli (EC 6.3.1.2) utilizes ammonia produced by nitrate reduction, amino acid degradation, and photorespiration.
    L-Glutamine Synthetase, Escherichia coli
  • HY-P2752A
    Lipoprotein Lipase, Bovine
    Lipoprotein lipase, Bovine (EC 3.1.1.34) belongs to the lipase gene family and is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins (such as those in chylomicrons and very low-density lipoproteins (VLDL)) into two free fatty acid molecules and one monoacylglycerol molecule. Lipoprotein also participates in promoting cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. Lipoprotein requires ApoC-II as a cofactor. Lipoprotein attaches to the luminal surface of capillary endothelial cells via glycosylphosphatidylinositol high-density lipoprotein-binding protein 1 (GPIHBP1) and heparan sulfate proteoglycan.
    Lipoprotein Lipase, Bovine
  • HY-P2752B
    Lipoprotein Lipase, Burkholderia sp.
    Lipoprotein Lipase, Burkholderia sp. (EC 3.1.1.34) belongs to the lipase gene family and is a water-soluble enzyme that hydrolyzes triglycerides in lipoproteins (such as those in chylomicrons and very low-density lipoproteins (VLDL)) into two free fatty acid molecules and one monoacylglycerol molecule. Lipoprotein also participates in promoting cellular uptake of chylomicron remnants, cholesterol-rich lipoproteins, and free fatty acids. Lipoprotein requires ApoC-II as a cofactor. Lipoprotein attaches to the luminal surface of capillary endothelial cells via glycosylphosphatidylinositol high-density lipoprotein-binding protein 1 (GPIHBP1) and heparan sulfate proteoglycan.
    Lipoprotein Lipase, Burkholderia sp.
  • HY-P2756A
    Alcohol Oxidase, Hansenula sp.
    Alcohol oxidase, Hansenula sp. (EC 1.1.3.13) is a redox enzyme that acts on the CH-OH group in donor molecules and uses oxygen as an acceptor. The two substrates of Alcohol Oxidase, Hansenula sp. (EC 1.1.3.13) are primary alcohols and O2, while its two products are aldehydes and H2O2.
    Alcohol Oxidase, Hansenula sp.
  • HY-P2756B
    Alcohol Oxidase, Pichia pastoris
    Alcohol Oxidase, Pichia pastoris (EC 1.1.3.13) is a redox enzyme that acts on the CH-OH group in donor molecules and uses oxygen as an acceptor. The two substrates of Alcohol Oxidase, Pichia pastoris (EC 1.1.3.13) are primary alcohols and O2, while its two products are aldehydes and H2O2.
    Alcohol Oxidase, Pichia pastoris
  • HY-P2759A
    Thioredoxin Reductase, E.coli
    Thioredoxin Reductase, E. coli (EC 1.8.1.9) is an E. coli-derived thioredoxin reductase (TrxR) that, compared to mammalian TrxR, lacks the redox active site-the C-terminal -Cys-SeCys-.
    Thioredoxin Reductase, E.coli
Cat. No. Product Name / Synonyms Application Reactivity