Biochemical Detection Enzymes

Alcohol oxidase is a functional enzyme of methanol utilization pathway and can be isolated from yeast peroxisome.

Hexokinase, Yeast is a hexokinase derived from yeast. Hexokinase, Yeast can be isolated from both fresh and dried baker's yeast. Hexokinases are evolutionarily conserved enzymes that phosphorylate six-carbon sugars (hexoses). Hexokinase prepares glucose for intracellular utilization. Hexokinase, Yeast is inhibited by 6-Deoxy-6-fluoroglucos.

Phospholipase A2 (PLA2) is a calcium-dependent, heat-stable enzyme that catalyzes the hydrolysis of glycerophospholipids at the sn-2 position of cellular membranes, thereby releasing Arachidonic Acid (AA) (HY-109590). Phospholipase A2 is a key mediator in the biosynthesis of pro-inflammatory lipid mediators, critically involved in inflammatory processes. Phospholipase A2 can be used for cardiovascular and inflammatory diseases research.

3-Hydroxybutyrate dehydrogenase (3-HBDH), a mitochondrial enzyme, is a key enzyme in the ketone body metabolism pathway. 3-Hydroxybutyrate dehydrogenase is the last enzyme for ketone synthesis in the liver and the first enzyme for ketone breakdown in extracellular tissues. The absence of 3-Hydroxybutyrate dehydrogenase leads to the inhibition of fatty acid oxidation in the liver during fasting in mice, resulting in lipid accumulation and the development of fatty liver.

Glyceraldehyde phosphate dehydrogenase (EC 1.2.1.12) is the target of anti-thymocyte and anti-apoptotic agents. Glyceraldehyde phosphate dehydrogenase catalyzes the chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals.

Hemicellulase is a hemicellulose-targeting hydrolase that breaks down the binding of glucose and polymers to water molecules present in plant fibers. Hemicellulase specifically degrades hemicellulose (such as xylan and mannan) in plant cell walls by hydrolyzing β-1,4-xylosidic bonds and ester bonds (such as acetyl and ferulic acid ester bonds). Hemicellulase relies on the synergistic action of the glycoside hydrolase (GH) and carbohydrate esterase (CE) families to achieve efficient hydrolysis through acid-base catalysis (such as Glu/Asp residues) and substrate binding pockets. Hemicellulase can be used in the food industry (such as improving bread texture)， biofuel production (lignocellulose pretreatment) and paper industry (biobleaching).

Acyl coenzyme A synthetase (ACS), namely acetyl coenzyme A synthetase, is often used in biochemical research. Acyl coenzyme A synthetase can catalyze the activation of fatty acids by coenzyme A through a two-step thioesterification reaction to produce acyl coenzyme A, and then participate in a variety of anabolic and catabolic lipid metabolism pathways, and participate in the TCA cycle in aerobic respiration.

Butyrylcholinesterase (BCHE), Horse Serum (BCHE, BuChE, PCHE, pseudocholinesterase, plasma cholinesterase, Acylcholine acyl-hydrolase, Choline esterase, butyryl) is a biological material or organic compound that can be used in life science research.

Sarcosine oxidase, Bacillus (SAO) can catalyze the oxidative demethylation of sarcosine to generate glycine, H₂O₂, 5,10-CH₂-tetrahydrofolate, which are often used in biochemical reactions.

Alkaline Phosphatase (Apase), Calf intestinal is an alkaline phosphatase from Calf intestinal, and is one of the most active alkaline phosphatases. Alkaline Phosphatase, Calf intestinal is an orally active membrane-bound glycoprotein that catalyzes the hydrolysis of phosphate monoesters at alkaline pH. Alkaline Phosphatase, Calf intestinal reduces myeloperoxidase activity and bacterial translocation. Alkaline Phosphatase, Calf intestinal improves survival rate of mice infected with E. coli. Alkaline Phosphatase, Calf intestinal improves TNBS-induced colon inflammation.

Protocatechuate 3,4-dioxygenase is a dioxygenase. Protocatechuate 3,4-dioxygenase belongs to the non-heme iron dioxygenase class. Protocatechuate 3,4-dioxygenase catalyzes the cleavage of the aromatic ring of 3,4-dihydroxybenzoate, attaching two atoms of molecular oxygen to the compound to generate β-carboxy-cis,cis-muconate. Protocatechuate 3,4-dioxygenase is a key enzyme in the β-ketoadipic acid pathway. It is found in marine bacteria associated with Roseobacter. Protocatechuate 3,4-dioxygenase can be isolated from Pseudomonas aeruginosa.

Creatininase, Microorganism (Creatinine amidohydrolase; CAH), namely creatinine amidohydrolase, from Pseudomonas putida, is a homohexameric enzyme commonly used in biochemical research. Creatininase acts on carbon-nitrogen bonds other than peptide bonds, and can catalyze the hydrolysis of creatinine to creatine, which can then be metabolized by creatinase to urea and sarcosine.

Aspartate aminotransferase (EC 2.6.1.1), porcine heart is a metabolic regulator with the highest activity in the heart, liver and skeletal muscle. Aspartate aminotransferase, porcine heart comprises two isozymes: the cytoplasmic form (AST1) and the mitochondrial form (AST2). By catalyzing reversible transamination reactions between oxaloacetate, L-glutamate and other substances, it is deeply involved in key physiological processes such as amino acid metabolism, the tricarboxylic acid cycle and neurotransmitter synthesis. Aspartate aminotransferase, porcine heart also provides substrate support for the synthesis of urea and purines/pyrimidines. Aspartate aminotransferase, porcine heart is a serum marker reflecting cardiac and hepatic injury, and its abnormal levels are also closely associated with myocardial infarction, cardiovascular diseases and various cancers.

Formate dehydrogenase is a class of oxidoreductases widely distributed in bacteria, fungi, plants and animals. Formate dehydrogenase catalyzes the reversible conversion between formic acid and carbon dioxide, accompanied by redox reactions of the coenzyme NAD⁺/NADH or other electron carriers.

Pyruvate Kinase, Microorganism (PK) is a glycolytic enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP.

L-Lactate dehydrogenase, E.coli is a redox enzyme. L-Lactate dehydrogenase, E.coli catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity.

Formaldehyde dehydrogenase is a widely occuring enzyme that can catalyze S-hydroxymethylglutathione in the presence of NAD. Formaldehyde dehydrogenase detoxifies formaldehyde within cells through capturing and limiting it from reaching a toxic level. Formaldehyde dehydrogenase can be studied in research on M. tuberculosis.

Recombinant myokinase, Rabbit muscle (Myokinase), is a phosphotransferase enzyme, is often used in biochemical studies. Recombinant myokinase, Rabbit muscle catalyzes the interconversion of adenosine phosphates. Recombinant myokinase, Rabbit muscle monitors phosphate nucleotide levels inside the cell, it plays an important role in cellular energy homeostasis.

5α-reductase, Rat (Sprague-Dawley) Liver is an enzyme involved in steroid metabolism and participates in the androgen metabolic pathway. 5α-reductase, Rat (Sprague-Dawley) Liver catalyzes the conversion of testosterone to 5α-dihydrotestosterone (DHT). DHT plays important roles in the development of male sex organs, hair growth, prostate function, and other aspects.

Beta-glucuronidase (bovine liver) is a glycoside hydrolase that hydrolyzes β-glucuronic acid and sulfate esters in urine and other biological fluids, thereby releasing β-glucuronides. Beta-glucuronidase (bovine liver) cannot effectively hydrolyze Estriol glucuronide. Beta-glucuronidase (bovine liver) can be used in studies related to systemic gangliosidosis.