Enzimi nelle Proteine Ricombinanti

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.

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.

Multi-copper oxidase from the family of polyphenol oxidades. It can be also found in many plants and bacteria. Laccase catalyses the oxidation of phenolic compounds such as lignin. It can oxidase non phenolic groups too with the use of mediators, chemical agents involved in the transfer of the electrons during the reaction. In some cases, laccase can also oxidise halogenated compounds. This enzyme is used for enzymatic assays, lignol screening tests and for waste water treatment to remove biodegrdable pollutants.

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.

Butyrylcholinesterase is an enzyme made in the liver and found mainly in blood plasma. Butyrylcholinesterase (EC 3.1.1.8), also known as BChE or BuChE, is a nonspecific cholinesterase enzyme that hydrolyses choline-based esters. One unit of Butyrylcholinesterase will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per minute at pH 8.0 and 37 °C.

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

Sulfatase from Helix pomatia is a highly potent enzyme that is capable of hydrolyzing sulfated compounds and sulfate esters. It has been widely used in various applications such as glucosinolate analysis, genistein extraction preparation, and regiospecificity studies. With a concentration of ≥10,000 units per gram of solid, this sulfatase offers exceptional enzymatic activity for sulfatase assays. It effectively catalyzes the hydrolysis of sulfated substrates, including p-nitrocatechol sulfate, naphthyl sulfate and phenyl sulfates.The enzyme can be incubated with the desired sample to facilitate the release of sulfate groups from sulfated compounds. Sulfatase from Helix pomatia is a valuable tool for researchers and scientists working in diverse fields requiring efficient and reliable enzymatic hydrolysis capabilities. Additionally the enzyme has been found to have industrial applications, such as in the bioconversion of industrial chemicals, where it can be used as a catalyst.

Expression system: HEK297 Cells<br>Length: 21-472, Full Length of Mature Protein<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-169, Partial<br>Activity: BLI

Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, is a potent activator of phosphofructokinase, which is a rate-limiting

GUCY2C Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Carbonic Anhydrase 9 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.

Protein phosphatase 1G, also known as Protein phosphatase 1C, Protein phosphatase 2C isoform gamma, Protein phosphatase magnesium-dependent 1 gamma, PP2C-gamma

Genetic engineers have used glutathione S-transferase to create the GST gene fusion system.

GUCY2C Protein, Canine, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

VEGFR3/FLT4 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.

ACE2/ACEH Protein, Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with hFc tag.

Cyclophilin A Protein, Human, Recombinant (His) is expressed in E.

Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which

Carboxypeptidase B2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Alpha-L-iduronidase is a glycoside hydrolase enzyme that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate.
This enzyme is supplied as a 2 mg/mL aqueous solution in 25 mM sodium acetate, 150 mM NaCl, 50% glycerol, pH 5.0 from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as lyophilisate (FA181881)

Peroxidase 12 recombinantly expressed in P. pastoria comes in a freeze-dried formulation. It has its pH optimum at 5-8 and temp. optimum at 20-40°C. Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. Peroxidase 12 was shown to act on styrene, veratryl alcohol, vanillyl alcohol, n-methyl anthranilate and thioanisole.

Lipase 68 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-9 and temp. optimum at 30°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 68 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (75 %), laurate (8 %), palmitate (1 %) and stearate (0.1 %).

Lipase 32 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 50-70°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 32 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (88 %), laurate (11 %), palmitate (0.3 %) and stearate (0.1 %).

Lipase Y 01 is an enzymatic catalyst, which is derived from microbial fermentation with a specific mode of action involving the hydrolysis of triglycerides into glycerol and free fatty acids. This enzyme operates by breaking ester bonds in fats, facilitating their breakdown and conversion into simpler molecules.

A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of > 6 months at 4-25°C can be guaranteed.
Key features are:

LacBuster® Settle Plates contain a general purpose growth medium (tryptone soya agar) supplemented with LacBuster®, a high-performing beta-lactamase to effectively neutralize beta-lactam antibiotics. The media plates are suitable for the cultivation of a wide variety of microorganisms in environmental monitoring within the pharmaceutical industry.

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.

LacBuster®-S 50 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 50 IU beta-lactamase II and 500 IU beta-lactamase I activity per vial.

Cholesterol dehydrogenase (EC 1.1.1.840) is NADP+-dependant oxidoreductase, that catalyses the following reaction:cholesterol + NADP+ + H2O → cholest-4-en-3-one + NADPH + H+This is achieved by oxidizing alcohol hydroxy-group into ketone. One unit of cholesterol dehydrogenase will produce 1.0 μmole of cholest-4-en-3-one per minute at pH 8.5 and 25 °C.

Lipase 16 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at >40°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 16 was shown to hydrolyze p-Nitrophenyl esters of butyrate (58 % activity compared to octanoate), octanoate (100 %), laurate (40 %), palmitate (27 %), stearate (13 %), arachidate (2 %) and behenate (0.2 %).

Endopeptidase, liquid, food grade, broad spectrum is an enzymatic product used in the food industry. It is derived from microbial sources, specifically engineered strains capable of producing high yields of proteolytic enzymes. This endopeptidase functions by hydrolyzing peptide bonds within proteins, targeting internal sites to break down long protein chains into smaller peptides and amino acids.

A proteolytic enzyme; degrades protein contaminants in nucleic acid preparations

Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.Spray dried version of EPLD840.6_R

Immobilized lipase is an advanced enzymatic product, which is derived from lipases, enzymes primarily sourced from microbial, plant, or animal origins. This product operates through a catalytic mechanism where the lipase is attached to a solid support, enhancing its stability and reusability in various reactions. This immobilization allows the enzyme to maintain activity over a wide range of conditions, including different pH levels and temperatures.

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 >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 %).

Lipase, powder, food-grade, broad spectrum is an enzyme product, which is derived from microbial sources such as fungi and bacteria through a fermentation process. This enzyme operates by catalyzing the hydrolysis of fats into free fatty acids and glycerol, facilitating the breakdown of complex lipid molecules.

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