Enzimas en Proteínas Recombinantes

<p>75u/mg - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) is an enzyme that catalyzes the following reaction:  glyceraldehyde 3-phosphate + NAD+ + Pi ⇌ glycerate 1,3-bisphosphate + NADH + H+  One unit of GAPDH will convert 1.0 μmole of glyceraldehyde 3-phosphate into glycerate 1,3-bisphosphate per minute at pH 8.5 and 37 °C in the presence of NAD+ and phosphate. NAD+ is available here.</p>

<p>α-Glucosidase is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues to produce α-D-glucose. This enzyme has been isolated from Bacillus stearothermophilus and is used as an industrial catalyst in the production of glucose syrups.  One Unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute under optimum conditions.</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>Maltose phosphorylase (systematic name maltose:phosphate 1-beta-D-glucosyltransferase; EC 2.4.1.8) is an enzyme that catalyzes the following reaction:  maltose + Pi ⇌ D-glucose + beta-D-glucose 1-phosphate  One unit of maltose phosphorylase will produce 1.0 μmole of D-Glucose from maltose per minute at pH 7.0 and 30°C.</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>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>Urokinase (urokinase-type plasminogen activator, uPA; EC 3.4.21.73) is as serine protease. Its physiological substrate is plasminogen. Urokinase converts plasminogen into an active enzyme, plasmin, which is also a serine protease. In its active form plasmin plays an important role in dissolving blood clots. Despite its name, Urokinase is not a kinase.</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>Invertase is an enzyme that catalyzes the hydrolysis of sucrose to glucose and fructose and can be found in plants and microorganisms</p>

<p>Acetylcholinesterase is an enzyme that breaks down acetylcholine</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>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>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>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>E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg</p>

<p>Lysozyme is a bacteriolytic enzyme, which is primarily derived from hen egg whites. It functions by hydrolyzing the β-1,4-glycosidic linkages in the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. This enzymatic activity results in the lysis and subsequent death of the bacterial cells, providing a potent antimicrobial effect.</p>

<p>Nucleoside phosphorylase (Purine nucleoside phosphorylase, PNP, PNPase, inosine phosphorylase, inosine-guanosine phosphorylase; EC 2.4.2.1) is an enzyme that catalyzes the following reaction:  purine nucleoside + Pi ⇌ purine + alpha-D-ribose 1-phosphate  One unit of nucleoside phosphorylase will phosphorylate 1.0 micromole of inosine to hypoxanthine and alpha-D-ribose 1-phosphate per min at pH 7.4 and 25°C.</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>Endo-β-1,4-Mannanase (other names Mannan endo-1,4-β-mannosidase, endo-β-1,4-mannase, β-mannanase B, β-1, 4-mannan 4-mannanohydrolase, endo-β-mannanase, β-D-mannanase, 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78) is an enzyme, catalyzing the hydrolysis of -1, 4-mannosidic linkages in mannans, glucomannans and galactomannans. One unit of Endo-β-1,4-Mannanase will release 1.0 µmole of mannose reducing-sugar per minute from a 3mg/ml mannan solution at pH 5.5 and 37degC.  Expressed in U/g.</p>

<p>Endoproteinase Glu-C (Glutamyl endopeptidase, V8 protease, GluV8, EC 3.4.21.19) is a protease that hydrolyzes peptide bonds at the carboxylic side of either exclusively Glu, or Glu and Asp residues, depending on the buffer conditions. One unit of endoproteinase Glu-C will generate 1.0 μmole of p-nitroaniline from Z-Phe-Leu-Glu-pNA peptide mimic substrate per minute at pH 7.8 and 25 °C. Z-Phe-Leu-Glu-pNA substrate is available here.molecular weight ~ 27000.</p>