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-P2869J
    β-Galactosidase, Kluyveromyces lactis
    β-Galactosidase, Kluyveromyces lactis is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. SubstRates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins.
    β-Galactosidase, Kluyveromyces lactis
  • HY-P2871C
    α-Galactosidase, positionally specific, Escherichia coli
    α-Galactosidase, positionally specific, Escherichia coli (EC 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Two recombinant forms of α-Galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN).
    α-Galactosidase, positionally specific, Escherichia coli
  • HY-P2871D
    α-Galactosidase, Clostridium cellulolyticum
    α-Galactosidase, Clostridium cellulolyticum (EC 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Two recombinant forms of α-Galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN).
    α-Galactosidase, Clostridium cellulolyticum
  • HY-P2871E
    α-Galactosidase, Cellvibrio mixtus
    α-Galactosidase, Cellvibrio mixtus (EC 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Two recombinant forms of α-Galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN).
    α-Galactosidase, Cellvibrio mixtus
  • HY-P2871H
    α-Galactosidase, Thermus brockianus
    α-Galactosidase, Thermus brockianus (EC 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. Two recombinant forms of α-Galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN).
    α-Galactosidase, Thermus brockianus
  • HY-P2871I
    α-Galactosidase, Green coffee beans
    α-Galactosidase, Green coffee beans (EC 3.2.1.22) is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
    α-Galactosidase, Green coffee beans
  • HY-P2872A
    Thioglucosidase, Sinapis alba (white mustard) seed
    Thioglucosidase, Sinapis alba (white mustard) seed (EC 3.2.1.147) hydrolyzes the S-glucosidic bond of a glucosinolate substrate to form an unstable aglycone that rearranges with the loss of sulfate primarily to the isothiocyanate, though thiocyanates and nitriles are also formed.
    Thioglucosidase, Sinapis alba (white mustard) seed
  • HY-P2877A
    Tannase, Aspergillus oryzae
    Tannase, Aspergillus oryzae (EC 3.1.1.20) catalyzes the hydrolysis of tannic acid to produce gallic acid and glucose.
    Tannase, Aspergillus oryzae
  • HY-P2878A
    Phosphodiesterase l, Rattlesnake venom 9025-82-5 98%
    Phosphodiesterase l, Rattlesnake venom (PDE, Rattlesnake venom) is a non-selective phosphodiester bond hydrolase targeting phosphodiester bonds in oligonucleotides, catalyzing their hydrolysis into mononucleotides. Phosphodiesterase l, Rattlesnake venom cleaves phosphodiester linkages in DNA fragments digested by DNase I. Phosphodiesterase l, Rattlesnake venom is promising for research of nucleic acid structure and metabolism.
    Phosphodiesterase l, Rattlesnake venom
  • HY-P2878B
    Phosphodiesterase I, Bothrops atrox
    Phosphodiesterase I, Bothrops atrox (EC 3.1.4.1) breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C.
    Phosphodiesterase I, Bothrops atrox
  • HY-P2878C
    Phosphodiesterase I, Crotalus atrox (Western Diamondback Rattlesnake)
    Phosphodiesterase I, Crotalus atrox (Western Diamondback Rattlesnake) (EC 3.1.4.1) breaks phosphodiester bonds and catalyzes the hydrolysis of various nucleotide polyphosphates. Phosphodiesterase I is released from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C.
    Phosphodiesterase I, Crotalus atrox (Western Diamondback Rattlesnake)
  • HY-P2879B
    Cholesterol esterase, Candida cylindracea 9026-00-0 98%
    Cholesterol esterase, Candida cylindracea is an enzyme located in the intestines that hydrolyzes cholesterol esters into cholesterol and free fatty acids. Also known as bile salt-stimulated lipase or carboxylester lipase, this enzyme facilitates cholesterol metabolism and absorption in the body. It can also be used as a biochemical reagent, and is employed in conjunction with cholesterol oxidase (HY-P2848) to measure cholesterol levels.
    Cholesterol esterase, Candida cylindracea
  • HY-P2879C
    Cholesterol esterase, schizophyllum commune 98%
    Cholesterol esterase, Schizophyllum commune is an enzyme that catalyzes the hydrolysis of cholesterol esters into free cholesterol and fatty acids, facilitating the absorption of cholesterol in the intestine. Cholesterol esterase, Schizophyllum commune can be used in combination with cholesterol oxidase to measure cholesterol content.
    Cholesterol esterase, schizophyllum commune
  • HY-P2879D
    Cholesterol esterase, Candida Rugosa 98%
    Cholesterol esterase, Candida Rugosa (EC 3.1.1.13), catalyzes the synthesis of sterols and fatty acids from sterol esters. In the presence of bile acids, it aggregates to form a hexamer, which may be the active form of this enzyme.
    Cholesterol esterase, Candida Rugosa
  • HY-P2888A
    Bilirubin oxidase, bacillus cereus 80619-01-8 98%
    Bilirubin oxidase, bacillus cereus is a multi-copper oxidase that catalyzes the oxidation of bilirubin into biliverdin, as well as other tetrapyrroles, phenols, and aryl diamines. Bilirubin oxidase, bacillus cereus can serve as a single-enzyme deoxygenator, catalyzing the direct reduction of oxygen to water in the presence of electron donor substrates, without releasing hydrogen peroxide. Bilirubin oxidase, bacillus cereus can be used to develop enzyme-based biosensors.
    Bilirubin oxidase, bacillus cereus
  • HY-P2888B
    Bilirubin oxidase, Magnaporthe oryzae 98%
    Bilirubin oxidase (BOD), Magnaporthe oryza is a multi-copper oxidase that catalyzes the oxidation of bilirubin to biliverdin and reduces molecular oxygen to water. Bilirubin oxidase, Magnaporthe oryzae can participate in the metabolism of porphyrin and chlorophyll, and is widely used in biochemical research as a catalyst for oxygen reduction.
    Bilirubin oxidase, Magnaporthe oryzae
  • HY-P2888C
    Bilirubin oxidase, Bacillus pumilus 98%
    Bilirubin oxidase (BOD), Bacillus pumilus is a multicopper oxidase that catalyzes the oxidation of bilirubin to biliverdin, as well as other tetrapyrrole, phenols, and aryl diamines. Bilirubin oxidase, Bacillus pumilus can serve as a single-enzyme deoxygenator, catalyzing the direct reduction of oxygen to water in the presence of electron donor substrates, without releasing hydrogen peroxide. Bilirubin oxidase, Bacillus pumilus can be used to develop enzyme-based biosensors.
    Bilirubin oxidase, Bacillus pumilus
  • HY-P2888D
    Bilirubin Oxidase, Myrothecium verrucaria
    Bilirubin Oxidase, Myrothecium verrucaria (EC 1.3.3.5) is a family of oxidoreductases that act on the CH-CH group as a donor and use oxygen as an acceptor. Bilirubin Oxidase, Myrothecium verrucaria (EC 1.3.3.5) is involved in the metabolism of porphyrins and chlorophyll. The two substrates of Bilirubin Oxidase, Myrothecium verrucaria (EC 1.3.3.5) are bilirubin and O2, while its two products are biliverdin and H2O.
    Bilirubin Oxidase, Myrothecium verrucaria
  • HY-P2889A
    Pyranose Oxidase, E. coli
    Pyranose Oxidase, E. coli (EC 1.1.3.10) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. Pyranose Oxidase is a homotetrameric protein that contains covalently bound flavin adenine dinucleotide (FAD).
    Pyranose Oxidase, E. coli
  • HY-P2890B
    Laccase, Trametes versicolor
    Laccase, Trametes versicolor (EC 1.10.3.2), is a blue copper oxidase that reduces molecular oxygen to water. Laccase can oxidize polyphenols, methoxylated phenolic compounds, and diamines, but not tyrosine. Laccase's oxidation reaction is a single-electron reaction and produces free radicals.
    Laccase, Trametes versicolor
Cat. No. Product Name / Synonyms Application Reactivity