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-P2931A
    Triosephosphate Isomerase, Rabbit
    Triosephosphate Isomerase, Rabbit (EC 5.3.1.1) catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. Triosephosphate Isomerase plays an important role in glycolysis and is essential for efficient energy production.
    Triosephosphate Isomerase, Rabbit
  • HY-P2931B
    Triosephosphate Isomerase, Baker's yeast (S. cerevisiae)
    Triosephosphate isomerase in Baker's yeast (S. cerevisiae) (EC 5.3.1.1) catalyzes the reversible interconversion between the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. Triosephosphate isomerase in Baker's yeast (S. cerevisiae) (EC 5.3.1.1) plays a crucial role in glycolysis and is essential for efficient energy production.
    Triosephosphate Isomerase, Baker's yeast (S. cerevisiae)
  • HY-P2950L
    α1-2,3 Mannosidase, Xanthomonas manihotis 98%
    α1-2,3 Mannosidase, Xanthomonas manihotis is an acid hydrolase which is located in plant vacuoles and is thought to be involved with the turnover of N-linked glycoproteins.
    α1-2,3 Mannosidase, Xanthomonas manihotis
  • HY-P2951A
    Phenylalanine Ammonia-Lyase, Rhodotorula glutinis
    Phenylalanine Ammonia-Lyase, Rhodotorula glutinis (EC 4.3.1.24) can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin.
    Phenylalanine Ammonia-Lyase, Rhodotorula glutinis
  • HY-P2952A
    Myokinase, Rabbit
    Myokinase, Rabbit (EC 2.7.4.3) for research on ATP metabolism and enzymatic activity.
    Myokinase, Rabbit
  • HY-P2952B
    Myokinase, Bacillus stearothermophilus
    Myokinase, Bacillus stearothermophilus (EC 2.7.4.3) for research on ATP metabolism and enzymatic mechanisms.
    Myokinase, Bacillus stearothermophilus
  • HY-P2952C
    Myokinase, Chicken
    Myokinase, Chicken (EC 2.7.4.3) for research on ATP metabolism and enzymatic mechanisms.
    Myokinase, Chicken
  • HY-P2952D
    Myokinase, Yeast 98%
    Myokinase, Yeast (EC 2.7.4.3) for research on ATP metabolism and enzymatic mechanisms.
    Myokinase, Yeast
  • HY-P2961A
    Glutathione-S-Transferase, Rat
    Glutathione-S-Transferase, Rat (EC 2.5.1.18) comprises a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification.
    Glutathione-S-Transferase, Rat
  • HY-P2964A
    L-Phenylalanine Dehydrogenase, Sporosarcina sp.
    L-Phenylalanine Dehydrogenase, Sporosarcina sp. (EC 1.4.1.20) is a member of a large family of amino-acid dehydrogenases, which has a two-domain, three-dimensional structure.
    L-Phenylalanine Dehydrogenase, Sporosarcina sp.
  • HY-P2972A
    Sulfatase, Aerobacter aerogenes
    Sulfatase, Aerobacter aerogenes (EC 3.1.6.1) is an esterase that catalyzes the hydrolysis of sulfate esters. Sulfatase, together with sulfotransferases, constitutes the main catalytic mechanism for the synthesis and hydrolysis of sulfate esters.
    Sulfatase, Aerobacter aerogenes
  • HY-P2972B
    Sulfatase, Abalone 98%
    Sulfatase, Abalone (EC 3.1.6.1) is an esterase that catalyzes the hydrolysis of sulfate esters. Sulfatase, together with sulfotransferases, constitutes the main catalytic mechanism for the synthesis and hydrolysis of sulfate esters.
    Sulfatase, Abalone
  • HY-P2972C
    Sulfatase, Patella vulgata (keyhole limpet) 98%
    Sulfatase, Patella vulgata (keyhole limpet) (EC 3.1.6.1) is an esterase that catalyzes the hydrolysis of sulfate esters. Sulfatase, together with sulfotransferases, constitutes the main catalytic mechanism for the synthesis and hydrolysis of sulfate esters.
    Sulfatase, Patella vulgata (keyhole limpet)
  • HY-P2974A
    Elastase, Rat
    Elastase, Rat (EC 3.4.21.35) is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta-barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together.
    Elastase, Rat
  • HY-P2983C
    Angiotensin Converting Enzyme, Bovine
    Angiotensin Converting Enzyme, Bovine (EC 3.4.15.1) increases blood pressure by causing blood vessels to constrict. Angiotensin Converting Enzyme, Bovine (EC 3.4.15.1) does that by converting angiotensin I to angiotensin II, which constricts the vessels.
    Angiotensin Converting Enzyme, Bovine
  • HY-P2985B
    Alanine aminotransferase, Human (E.coli) 9000-86-6 98%
    Alanine aminotransferase, Human (E.coli) is a pyridoxal enzyme that catalyzes the reversible interconversion of L-alanine and 2-oxoglutalate to pyruvate and L-glutamate.
    Alanine aminotransferase, Human (E.coli)
  • HY-P2986A
    D-Amino Acid Oxidase, Porcine
    D-Amino Acid Oxidase, Porcine (EC 1.4.3.3) is used in the measurement of D-alanine and FAD, and in the preparation of L-amino acids from racemic mixtures.
    D-Amino Acid Oxidase, Porcine
  • HY-P2986B
    Apo D-Amino Acid Oxidase, Porcine
    Apo D-Amino Acid Oxidase, Porcine (EC 1.4.3.3) is entirely present as a monomeric protein.
    Apo D-Amino Acid Oxidase, Porcine
  • HY-P2988C
    α2-3,6,8,9 Neuraminidase, Arthrobacter ureafaciens
    α2-3,6,8,9 Neuraminidase, Arthrobacter ureafaciens (EC 3.2.1.18) catalyzes the hydrolysis of all linear and branched non-reducing terminal sialic acid residues from glycoproteins and oligosaccharides.
    α2-3,6,8,9 Neuraminidase, Arthrobacter ureafaciens
  • HY-P2988D
    α2-3,6,8 Neuraminidase, Clostridium perfringens
    α2-3,6,8 Neuraminidase, Clostridium perfringens is a glycoside hydrolase enzyme that cleave the glycosidic linkages of neuraminic acids.
    α2-3,6,8 Neuraminidase, Clostridium perfringens
Cat. No. Product Name / Synonyms Application Reactivity