Enzymes in Recombinant Proteins

α-Glucosidase (EC 3.2.1.20) 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.

Lysozyme, lyophilized powder, min 45000 FIP U/mg, is an enzymatic product derived primarily from egg white. It is a versatile and potent enzyme known for its ability to hydrolyze the β(1-4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. This mechanism of action is particularly effective against Gram-positive bacteria due to the accessibility of their peptidoglycan layer.

Protein kinase LATS2 is a serine/threonine kinase, which is a crucial component sourced intrinsically from cellular kinase cascades involved in cell regulation. This protein kinase is pivotal in the Hippo signaling pathway, which regulates cell growth, apoptosis, and stem cell renewal. LATS2 is part of the core kinase cascade that, upon activation, phosphorylates and inhibits the activity of the transcriptional co-activators YAP and TAZ, thereby controlling their transcriptional activity. This inhibition is key to maintaining proper cell proliferation and preventing uncontrolled cell growth that could lead to tumorigenesis.

LacBuster™-S 5000 is an enzymatic product, specifically a beta-lactamase, which originates from microbial sources known for their ability to produce enzymes that break down antibiotics. This product functions by hydrolyzing the beta-lactam ring of relevant antibiotics, thereby neutralizing their antibacterial activity.

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 %).

Enzyme involved in the reduction of hydrogen peroxide to water and oxygen. This is a highly important reaction as it protects the cell from oxidative damage.

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.

Tyrosinase (EC 1.14.18.1) is an enzyme that oxydises phenol derivatives (e.g. tyrosine, dopamine). One unit of tyrosinase dissolved in 3mL reaction mixture will cause the absorbance at 280nm to increase by 0.001 in the presence of L-tyrosine at pH 6.5 and 25 °C. L-tyrosine is available here.Lyophilized, from mushroom. Activity ≥1000 unit/mg

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 .

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.

Cell wall enzyme

Ultra nuclease (EC 3.1.30.2) is an enzyme that digests DNA and RNA in any form: single- and double-stranded, linear, circular and supercoiled. The ultimate reaction product is 5'-monophosphate oligonucleatides that are mostly three, four and five bases long. Please enquire for more information about Ultra nuclease, liquid, recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page

Lipase CR 02 is a high-purity enzyme preparation, which is derived from the microbial fermentation of selected fungal strains. With a mechanism involving the hydrolysis of ester bonds in lipids, Lipase CR 02 facilitates the conversion of triglycerides into glycerol and free fatty acids. This catalytic activity positions it as an essential tool in various biochemical and industrial applications.

Amidase is a hydrolase acting on carbon-nitrogen bonds in linear amides, and can be used in hydrolysis of amides to acids. Amidase 01 is of bacterial origin (P. aeruginosa) and has been produced in E.coli.

Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine  One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.

Lipase 01 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 25-45°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 01 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (57 %), laurate (13 %), palmitate (9 %), stearate (6 %), arachidate (2 %) and behenate (0.1 %).

Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industries