1. Metabolic Disease

Metabolic Disease

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-P2759B
    Thioredoxin Reductase (NADPH), Yeast
    Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.
    Thioredoxin Reductase (NADPH), Yeast
  • HY-P2763A
    β-Glucanase 2(thermostable)
    β-Glucanase 2(thermostable) is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). β-Glucanase 2 (thermostable) is an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose.
    β-Glucanase 2(thermostable)
  • HY-P2763B
    β-Glucanase 1(thermostable)
    β-Glucanase 1(thermostable) is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). β-Glucanase 1 (thermostable) is an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose.
    β-Glucanase 1(thermostable)
  • HY-P2765B
    Glyceraldehyde-3-phosphate Dehydrogenase, Rabbit
    Glyceraldehyde-3-phosphate Dehydrogenase, Rabbit (EC 1.2.1.12) catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis.
    Glyceraldehyde-3-phosphate Dehydrogenase, Rabbit
  • HY-P2765C
    Glyceraldehyde-3-phosphate Dehydrogenase, Chicken
    Glyceraldehyde-3-phosphate Dehydrogenase, Chicken (EC 1.2.1.12) catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis.
    Glyceraldehyde-3-phosphate Dehydrogenase, Chicken
  • HY-P2765D
    Glyceraldehyde-3-phosphate Dehydrogenase, Human
    Glyceraldehyde-3-phosphate Dehydrogenase, Human (EC 1.2.1.12) catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis.
    Glyceraldehyde-3-phosphate Dehydrogenase, Human
  • HY-P2766A
    Trehalase, Microorganism 9025-52-9 98%
    Trehalase, Microorganism (EC 3.2.1.28) is a trehalase that can effectively degrade trehalose in some bacteria. Trehalase, Microorganism can be used as a marker for acute kidney injury caused by proximal tubule damage.
    Trehalase, Microorganism
  • HY-P2766B
    Trehalase, Porcine
    Trehalase, Porcine (EC 3.2.1.28) is a glycoside hydrolase enzyme located in on the brush border of the small intestine that catalyzes the conversion of trehalose to glucose.
    Trehalase, Porcine
  • HY-P2768A
    Leucine dehydrogenase, Bacillus sp.
    Leucine dehydrogenase, Bacillus sp. (EC 1.4.1.9) is a carboxyl lyase that cleaves carbon-carbon bonds. L-Arginine Decarboxylase has one substrate, L-arginine, and two products, guanidine and CO2.
    Leucine dehydrogenase, Bacillus sp.
  • HY-P2770A
    β-Amylase, Sweet potato
    β-Amylase, Sweet potato (EC 3.2.1.2) hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units.
    β-Amylase, Sweet potato
  • HY-P2770B
    β-Amylase, Barley
    β-Amylase, Barley (EC 3.2.1.2) hydrolyzes the α-(1,4) glucan bonds in polysaccharides composed of three or more α-(1,4)-linked D-glucan units. In the absence of a reducing agent, β-Amylase, Barley (EC 3.2.1.2) rapidly polymerizes via thiol groups.
    β-Amylase, Barley
  • HY-P2771A
    Pectinesterase, Orange peel
    Pectinesterase, Orange peel (EC 3.1.1.11) catalyzes the hydrolysis of the methyl esters of pectin to yield pectate and methanol.
    Pectinesterase, Orange peel
  • HY-P2775A
    β-Glucosidase(thermostable)
    β-Glucosidase(thermostable) is a glucosidase enzyme located in on the brush border of the small intestine that acts upon β1->4 bonds linking two glucose or glucose-substituted molecules (i.e., the disaccharide cellobiose). β-Glucosidase(thermostable) is an exocellulase with specificity for a variety of beta-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of glucose.
    β-Glucosidase(thermostable)
  • HY-P2775B
    β-Glucosidase, Rhizobium etli
    β-Glucosidase, Rhizobium etli (EC 3.2.1.21), is a glucosidase that acts on the β1→4 glycosidic bond connecting two glucose molecules or glucose-substituted molecules (e.g., disaccharide cellobiose). β-Glucosidase is an exonuclease specific for a variety of β-D-glycosidic substrates. β-Glucosidase catalyzes the hydrolysis of the terminal non-reducing residues of β-D-glucosides, releasing glucose.
    β-Glucosidase, Rhizobium etli
  • HY-P2775C
    β-Glucosidase, Clostridium thermocellum
    β-Glucosidase, Clostridium thermocellum (EC 3.2.1.21), is a glucosidase that acts on the β1→4 glycosidic bond connecting two glucose molecules or glucose-substituted molecules (e.g., disaccharide cellobiose). β-Glucosidase is an exonuclease specific for a variety of β-D-glycosidic substrates. β-Glucosidase catalyzes the hydrolysis of the terminal non-reducing residues of β-D-glucosides, releasing glucose.
    β-Glucosidase, Clostridium thermocellum
  • HY-P2775D
    β-Glucosidase, Bacteroides fragilis
    β-Glucosidase, Bacteroides fragilis (EC 3.2.1.21), is a glucosidase that acts on the β1→4 glycosidic bond connecting two glucose molecules or glucose-substituted molecules (e.g., disaccharide cellobiose). β-Glucosidase is an exonuclease specific for a variety of β-D-glycosidic substrates. β-Glucosidase catalyzes the hydrolysis of the terminal non-reducing residues of β-D-glucosides, releasing glucose.
    β-Glucosidase, Bacteroides fragilis
  • HY-P2776C
    Hexokinase, Saccharomyces cerevisiae
    Hexokinase, Saccharomyces cerevisiae (EC 2.7.1.1), is a naturally occurring *Saccharomyces cerevisiae* hexokinase used in studies of glucose metabolism and enzymatic mechanisms.
    Hexokinase, Saccharomyces cerevisiae
  • HY-P2776D
    Hexokinase, Rhodothermus obamensis
    Hexokinase, Rhodothermus obamensis (EC 2.7.1.1), is a naturally occurring *Saccharomyces cerevisiae* hexokinase used in studies of glucose metabolism and enzymatic mechanisms.
    Hexokinase, Rhodothermus obamensis
  • HY-P2782A
    Chloramphenicol Acetyltransferase, Escherichia coli
    Chloramphenicol Acetyltransferase, Escherichia coli is a bacterial enzyme that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. Chloramphenicol Acetyltransferase, Escherichia coli covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. A histidine residue, located in the C-terminal section of Chloramphenicol Acetyltransferase, Escherichia coli, plays a central role in its catalytic mechanism.
    Chloramphenicol Acetyltransferase, Escherichia coli
  • HY-P2801A
    Glucose-6-Phosphatase, Rabbit
    Glucose-6-Phosphatase, Rabbit (EC 3.1.3.9) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins.
    Glucose-6-Phosphatase, Rabbit
Cat. No. Product Name / Synonyms Application Reactivity