Enzyme

<p>Myokinase (Adenylate kinase, EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction:ATP + AMP ⇌ 2 ADPOne unit of Myokinase will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at 25°C and pH 7.5.</p>

<p>Lyticase is a lysing enzyme that is designed to lyse cells in a biological sample. It contains an optimized wild-type guanine nucleotide-binding protein and has been shown to have high enzyme activities. Lyticase has also been shown to be active against opportunistic fungal strains, such as Candida glabrata, by disrupting their cell membranes. Lyticase is classified as a signal peptide with nuclear DNA, which allows it to be used in wastewater treatment applications. The enzyme can also be used for the analysis of the Toll-like receptor (TLR) response of microbes due to its electrochemical impedance spectroscopy properties.</p>

<p>hCAI/II-IN-6 is a selective and orally active inhibitor of human carbonic anhydrase (CA).</p>

<p>Cocarboxylase hydrochloride is a coenzyme derivative, which is primarily sourced from thiamine (vitamin B1). It plays a crucial role in biochemical processes by facilitating the enzymatic decarboxylation of alpha-keto acids within the cellular environment. This action is fundamental in energy production as it aids in the conversion of pyruvate to acetyl-CoA, subsequently entering the citric acid cycle. Cocarboxylase hydrochloride’s involvement in carbohydrate metabolism is especially vital for tissues with high metabolic rates, such as the heart and brain.</p>

<p>Glucosidases are enzymes belonging to the family of oxidoreductases. They catalyse the hydrolysis of starches to simple sugars. Glucosidase is widely used in the food, carbohydrate and biofuels industries. In recent years, its applicability has expanded to biotechnology for its potential application in bioenzymatic fuel cells.</p>

<p>Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids by degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.</p>

<p>Choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the following reaction: choline + O2 + H20 ⇌ betaine aldehyde + H2O2One unit of choline oxidase will form 1 μmole of H2O2 by oxidizing choline to betaine aldehyde per min at pH 8.0 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.</p>

<p>Glucose Dehydrogenase is an enzyme, which is typically derived from microbial sources such as bacteria and fungi. It functions by catalyzing the oxidation of glucose to gluconolactone, concurrently reducing a cofactor such as NAD⁺ or PQQ. This biochemical reaction is critical in various analytical applications due to its specificity and efficiency in glucose detection.Glucose Dehydrogenase is widely employed in the development of biosensors and diagnostic assays. Its primary application is in blood glucose monitoring devices, where its ability to accurately quantify glucose levels is crucial for managing diabetes. Additionally, it is utilized in research and development settings for biochemical assays that require precise glucose measurements. The enzyme's rapid and specific action on glucose molecules makes it an indispensable tool in both clinical and laboratory environments, contributing to advancements in biosensing technologies and metabolic studies.</p>

<p>D-Alanine aminotransferase (L-glutamic-pyruvic transaminase; EC 2.6.1.21) is an enzyme that catalyzes the following reaction:  D-alanine + α-ketoglutarate ⇌ pyruvate + D-glutamate  Please enquire for more information about D-Alanine Aminotransferase, Bacilus subtilis, Recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.</p>

<p>Superoxide dismutase is an enzyme that catalyzes the conversion of harmful superoxide into hydrogen peroxide and oxygen.</p>

<p>Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.</p>

<p>DNase I (Deoxyribonuclease I, EC 3.1.21.1) is an endonuclease that cleaves DNA, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3'. On average it produces tetranucleotides. One unit of the DNase I will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at 25°C.</p>

<p>Carbonic anhydrase inhibitor 6 is an hCA inhibitor that inhibits hCA IX, hCA II, hCA XII, and hCA I. It is used in the study of lupus erythematosus.</p>

<p>A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyprotein</p>

<p>Compound 1e, also known as ALP/Carbonic anhydrase-IN-1, is a dual inhibitor targeting both carbonic anhydrase (CA) isozymes II, IX, and XII, as well as alkaline</p>

LX-1031 is an effective inhibitor of tryptophan 5-hydroxylase. LX-1031 decreases serotonin (5-HT) synthesis peripherally.

Sezolamide hydrochloride is a potent topical carbonic anhydrase inhibitor.

Sezolamide is a carbonic anhydrase inhibitor.

<p>Diethyl-pythiDC is an collagen prolyl 4-hydroxylase inhibitor.</p>