Enzymes in Recombinant Proteins

<p>Penase (Penicillinase) is an enzyme, which is a type of β-lactamase sourced from various bacterial strains capable of deactivating penicillin. It accomplishes this by targeting the β-lactam ring, a crucial structural component of penicillin antibiotics, and hydrolyzing it, thereby neutralizing the antibiotic effect. This enzymatic action is a defense mechanism employed by certain bacteria to survive in environments saturated with penicillin-based antibiotics.</p>

<p>Please enquire for more information about Horseradish Peroxidase 01, rekombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Lipase 38 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at &gt;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 38 was shown to hydrolyze p-Nitrophenyl esters of acetate (27 % activity compared to butyrate), butyrate (100 %), octanoate (9 %) and caprate (5 %).</p>

<p>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.</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>Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is an enzyme that catalyses the following reaction:  2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O  One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per minute.</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 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°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 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).</p>

<p>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.</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>Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP &lt;71&gt;) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.beta lactamase I activity - min. 25.0 IU/mLbeta lactamase II activity - min. 10.0 IU/mL</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>Proteinase K, freeze-dried, recombinant is an enzyme preparation used extensively in molecular biology and biochemistry. It is derived through recombinant DNA technology, producing a highly pure enzyme that is expressed in a non-pathogenic host. Its mode of action involves the non-specific cleavage of peptide bonds in proteins, making it a critical tool for protein digestion.</p>

<p>CalB 02 is a lipase enzyme, which is a biocatalyst derived from the yeast Candida antarctica. It functions primarily by catalyzing the hydrolysis of ester bonds. This enzymatic action is due to the unique structure of the active site, which allows for precise substrate specificity and stereoselectivity.</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>CalB 10 is an industrial enzyme, specifically a lipase, which is derived from microbial sources, most commonly expressing the lipase B from Candida antarctica. It operates through the hydrolysis of ester bonds in lipids, enabling the conversion of triglycerides into glycerol and free fatty acids. This catalytic action is facilitated via its active site, where the nucleophilic serine residue attacks the carbonyl carbon of the substrate, forming a tetrahedral intermediate that eventually results in bond cleavage and product release.</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>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>Alpha Amylase is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C.</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>Lipase 70 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°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 70 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (62 %), laurate (15 %), palmitate (4 %), stearate (3 %), arachidate (2 %) and behenate (0.2 %).</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>Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP &lt;71&gt;) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.</p>

<p>Xylanase (Endo-1,4-β-xylanase, 1,4-β-D-Xylanxylanohydrolase, systematic name 4-β-D-xylan xylanohydrolase; EC 3.2.1.8) is an enzyme that digests polysaccharide xylan by hydrolyzing (1→4)-β-D-xylosidic linkages. One unit of Xylanase will hydrolyze 1.0 μmole of chromogenic substrate mimic per minute (available here) under optimal reaction conditions.</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>LacBuster™-S 50 is a beta-lactamase formulation, which is an enzyme of microbial origin with the ability to hydrolyze beta-lactam antibiotics. This enzymatic product is derived from specific bacterial species known for their resistance mechanisms, providing a robust capability to deactivate compounds such as penicillins and cephalosporins. Its mode of action involves the cleavage of the beta-lactam ring, a crucial structural component of these antibiotics, effectively neutralizing their antibacterial properties.</p>

<p>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.</p>

<p>Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°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 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).</p>

<p>DNA ligase (ATP) is an enzyme (EC 6.5.1.1) that ligates DNA strands, repairing nicks in double-standed DNA and coupling blunt-ended or cohesive DNA fragments. It requires 3′ hydroxyl and 5′ phosphate nucleoside ends for ligation and ATP as a cofactor.</p>

<p>LacBuster™-S 2000 is an enzyme preparation, specifically a beta-lactamase, which is derived from bacterial sources known for their capacity to degrade beta-lactam antibiotics. Through hydrolytic cleavage of the beta-lactam ring, this enzyme neutralizes the efficacy of beta-lactam antibiotics, thereby rendering them inactive.</p>

<p>Please enquire for more information about Nicotinamide phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</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>Please enquire for more information about Ribokinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Hypoxanthine phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acid</p>

<p>Please enquire for more information about Phosphoribosyl pyrophosphate synthase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Sucrose phosphorylase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Endoglycosidase H (systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96) is a highly specific enzyme, that cleaves asparagine-linked mannose rich oligosaccharides. One unit of Endoglycosidase H will remove &gt;95% of the carbohydrate from 10μg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10μl.The product EEH01.7 is available as a large-scale bulk supply of liquid enzyme solution and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.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>Please enquire for more information about Dextran dextrinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Porcine liver esterase (EC 3.1.1.1) is an enzyme that catalyses ester hydrolysis, producing a fatty acid and an alcohol. One unit of esterase will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 and 25 °C. Ethyl butyrate is available here.</p>

<p>β-Glucuronidase (EC 3.2.1.31) is an enzyme that hydrolyzes glucuronides. It can also be used to cleave benzodiazepine and steroid conjugates. One unit of β-Glucuronidase will hydrolyze a chromogenic substrate mimic 4-nitrophenyl-β-D-glucuronide to produce 1.0 μmole of 4-nitrophenol per minute at pH 5.0 and 37 °C.</p>

<p>L-Leucine dehydrogenase (Leucine dehydrogenase, systematic name L-leucine:NAD+ oxidoreductase (deaminating); EC 1.4.1.9) is an enzyme that catalyzes the following reaction:  L-leucine + H2O + NAD+ ⇌ 4-methyl-2-oxopentanoate + NH3 + NADH + H+  One unit of L-Leucine dehydrogenase will convert 1.0 µmole of L‑leucine into 4-methyl-2-oxopentanoate per min at pH 10.5 and 37 °C in the presence of NAD+. The enzyme requires NAD+ as a cofactor, it is available here.</p>

<p>Please enquire for more information about Superoxide dismutase, porcine erythrocytes including the price, delivery time and more detailed product information at the technical inquiry form on this page</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>20mg/ml aq. solution.  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 but 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>Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°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 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).</p>