Enzyme

Xylanase is an enzymatic product, which is typically derived from microbial sources such as fungi or bacteria. Its primary function involves catalyzing the hydrolysis of xylan, a major hemicellulose component found in plant cell walls. Through breaking down xylan into xylose and other oligosaccharides, xylanase significantly modifies plant material structure.

Cellulase, powder is an enzymatic product derived from microbial fermentation, specifically sourced from fungi or bacteria known for their cellulolytic activity. Cellulase acts by catalyzing the hydrolysis of cellulose, breaking it down into smaller polysaccharides and glucose. This decomposition occurs through synergistic action by three main components: endoglucanases, exoglucanases, and β-glucosidases, each targeting specific bonds in the cellulose structure, resulting in its complete breakdown.

PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as a large-scale bulk supply of liquid enzyme solution. See our PNGase F available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution.Also available is our endoH enzymes (EEH01.3 - research quantities and EEH01.7 - large scale bulk supply).

Heat Labile Uracil-DNA Glycosylase, 500 units, is an enzyme designed for molecular biology applications, primarily derived from a recombinant bacterial source. This enzyme effectively removes uracil from DNA molecules at temperatures that preserve the integrity of the DNA. With its heat-labile properties, the enzyme can be inactivated at moderately elevated temperatures, making it ideal for processes that require precise control over enzyme activity.

PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution . See our large-scale bulk supply of PNGase F for the deglycosylation of proteins in manufacture.Also available is our endoH enzymes (EEH01.3 - vials for research and EEH01.7 - large scale bulk supply).

Beta-lactamase enzymes demonstrate activity against clinically relevant beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. This product may be of particular interest for laboratory teams who require the sterility testing of biological specimens or for environmental monitoring applications.

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

Endoglycosidase H (Endo H) is a highly specific enzyme that cleaves N-linked oligosaccharides from glycoproteins, targeting high-mannose and certain hybrid-type N-glycans. It does not act on complex-type N-glycans, which are typically processed further in the Golgi apparatus. Due to its specificity, Endo H is widely used in research to study intracellular protein trafficking and post-translational modifications, particularly those occurring during glycoprotein maturation.This product is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solutionSee our EndoH (EEH01.7) available for large-scale bulk supply of liquid enzyme solution for the deglycosylation of proteins in manufacture.For removal of all N-linked carbohydrates from proteins see Cymit Quimica's PNGase F enzymes (PNG01.3 - vials for research and PNG01.7 - large-scale bulk supply)

Lipase 64 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 40-50°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 64 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (0.5 %) and laurate (0.1 %).

Cocarboxylase tetrahydrate is a coenzyme form of vitamin B1; cofactor for enzymes involved in carbohydrate catabolism

Fructose-6-phosphate kinase (Phosphofructokinase, PFK, EC 2.7.1.11) is an enzyme that catalyzes the following reaction:  F6P + ATP ⇌ F1,6BP + ATP  One unit of PFK will convert 1.0 μmole of fructose 6-phosphate and ATP to fructose 1,6-diphosphate and ADP per minute at pH 9.0 at 30 °C.

Glucose oxidase is an enzyme thata catalyses the rapid conversion of glucose into non-fermentable gluconic acid in the presence of oxygen (O2). Its used is widely expanded with many applications in the chemical and pharmaceutical industry, food and beverage, clinical studies and biotechnology, among others. It medical diagnosis, glucose oxidase serves as a biosensor for detecting and determining the different levels of glucose in blood samples.

Porcine pancreatic lipase is an enzyme that has been shown to have antioxidative properties. It is used as an additive in biodiesel production, where it prevents the formation of trans fatty acids and reduces the amount of free radicals. This enzyme has been shown to have lipase, protease, and amylase activities by using surface methodology. Porcine pancreatic lipase can be used for the treatment of autoimmune diseases such as multiple sclerosis and rheumatoid arthritis. This enzyme interacts with other enzymes such as lipases, proteases, and amylases to catalyze reactions on surfaces. It can be used for asymmetric synthesis by hydrogen bonding or by forming an intermediate complex with metal ions.

Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.

A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufacture

A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufacture

Luciferase enzyme from Photinus pyralis (firefly), which catalyzes the oxidation of firefly luciferin. This reaction depends on the presence of oxygen and ATP and causes the bioluminescence seen in fireflies