Enzyme

<p>Lipase 15 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 25°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 15 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (13 %), laurate (1 %), palmitate (1 %), stearate (&lt;1 %), arachidate (&lt;1 %) and behenate (&lt;1 %).</p>

<p>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.</p>

<p>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.</p>

<p>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 (&gt;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)</p>

<p>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 %).</p>

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

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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</p>

<p>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</p>

<p>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</p>

<p>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</p>

<p>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</p>

<p>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.</p>

<p>Lipase 44 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-10 and temp. optimum at 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 44 was shown to hydrolyze p-Nitrophenyl esters of butyrate (70 % activity compared to octanoate), octanoate (100 %), laurate (88 %), palmitate (6 %) and stearate (2 %).</p>

<p>Phosphoenolpyruvate carboxylase is an enzyme, often found naturally in the cytosol of plant cells, which is derived primarily from various plant species. It plays a crucial role in the photosynthetic process, particularly in C4 and CAM plants. By catalyzing the irreversible carboxylation of phosphoenolpyruvate (PEP) to oxaloacetate, this enzyme facilitates the fixation of carbon dioxide, a vital step in the conversion of carbon dioxide into organic compounds during photosynthesis.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Lipase 03 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 20-50°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 03 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (90 %), laurate (28 %), palmitate (14 %), stearate (9 %), arachidate (2 %) and behenate (3 %).</p>

<p>Phytate 1-phosphatase is a phosphatase enzyme that cleaves orthophosphate groups from phytic acid's inositol ring. This releases inorganic phosphate.</p>

<p>Dihydrofolate reductase (DHFR, 1.5.1.3) is a NADP+/NADPH-dependent oxidoreductase, that reduces dihydrofolate to tetrahydrofolate in the following reaction: dihydrofolate + NADPH + H+ ⇌ tetrahydrofolate + NADP+One unit of dihydrofolate reductase will convert 1.0 μmole of dihydrofolic acid into tetrahydrofolic acid in 1 minute at pH 7.5, 22°C and presence of NADPH.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>3-Oxo-5β-steroid Δ4-dehydrogenase is an enzyme crucial in the metabolic pathway of steroid hormones, facilitating the conversion of androgens and estrogens. It is predominantly found in the liver, but also in other tissues where steroid biosynthesis occurs. This enzyme catalyzes the dehydrogenation at the Δ4 position of 3-oxo-5β-steroids, playing a significant role in the modulation and regulation of steroid hormone levels within cells.</p>

<p>This product shows beta-lactamase 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.</p>

<p>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.</p>

<p>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.</p>

<p>Sphingomyelinase (SMase, Sphingomyelin phosphodiesterase, systematic name sphingomyelin cholinephosphohydrolase; EC 3.1.4.12) is an enzyme that hydrolyses sphingomyelin into phosphocholine and ceramide. One unit of sphingomyelinase will hydrolyze 1.0 µmole of chromogenic substrate analogue per minute at pH 7.4 and 37 °C.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Lipase 30 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 5.5-8 and temp. optimum at &gt;55°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 30 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (72 %), laurate (38 %), palmitate (7 %) and stearate (2 %).</p>

<p>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.</p>

<p>In a single vial and in a single step, the X-ShiningTM all-in-one ATP Assay provides an optimized reaction solution for the specific bioluminescent detection of ATP.  Simply reconstitute, and the X-ShiningTM all-in-one ATP Assay solution can be directly applied to samples for ATP measurement in a 1:1 ratio for an immediate bioluminescent read-out. The measurement of ATP levels is crucial to study cell cultures, cell viability, cell response, biochemical processes, to monitor environmental sample activity levels, to assess water quality, to test for biological contamination and to assess biocide efficacy. The X-ShiningTM all-in-one ATP Assay provides sufficient reagent solution to perform 50-to-100 measurements in a 96-well plate and can be easily adapted to measurements in tubes. Find out more about our innovative X-ShiningTM range here X-Shining | Innovation | Cymit Quimica .</p>

<p>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.</p>

<p>Dextranase (alternative names dextran hydrolase, endo-dextranase, endodextranase, dextranase DL 2, α-D-1,6-glucan-6-glucanohydrolase, 1,6-α-D-glucan 6-glucanohydrolase, EC 3.2.1.11) is dextran-degrading enzyme that hydrolyzes the α(1→6) glycosidic linkage of dextran, cutting it into progressively shorter fragments, ultimaly producing isomaltose (a disaccharide) and glucose. One unit of dextranase will cleave dextrane to yield 1.0 μmole of isomaltose per min at pH 6.0 and 37 °C.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Carboxypeptidase B is an enzyme responsible for the cleavage of arginine and lysine from a peptide's C-terminus</p>

<p>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.</p>

<p>A trypsin product which can be used as a standard in proteomics procedures such as mass spectrometry. Trypsin (EC 3.4.21.4) is a protease that hydrolyses proteins by cleaving the peptide bond at the carboxyl side of the positively charged amino acid (Lysine or Arginine). Trypsin belongs to a family of serine proteases, as it has a serine in its active site. Trypsin can be inhibited by using trypsin inhibitor Alpha 1 Antitrypsin.</p>

<p>Pyruvate oxidase is a phosphorylating oxidoreductase which uses FAD as a cofactor to convert pyruvate into acetate and CO2. Pyruvate oxidase (PoxB) is used in metabolism studies in bacteria and in clinical assays for pyruvate, and requires thiamine pyrophosphate (TPP) and magnesium alongside FAD for optimum activity.</p>

<p>Aspartate Aminotransferase (AST), Recombinant is a purified enzyme product utilized extensively in biochemical research and clinical diagnostics. Derived from a recombinant source, this enzyme mirrors the naturally occurring AST found in human tissues, ensuring consistency and reliability in experimental setups.</p>