Enzima

<p>α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues (e.g. in starch or oligosaccharides)  to produce α-D-glucose. 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 at pH 6.8 and 37 °C.</p>

<p>Urokinase (urokinase-type plasminogen activator, uPA; EC 3.4.21.73) is as serine protease. Its physiological substrate is plasminogen. Urokinase converts plasminogen into an active enzyme, plasmin, which is also a serine protease. In its active form plasmin plays an important role in dissolving blood clots. Despite its name, Urokinase is not a kinase.</p>

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.

The main protease Mpro is a key protein in the lifecycle of the SARS-CoV-2 virus. Mpro cleaves the viral polyproteins at the C-terminal end of a glutamine residue in recognition sequences containing Leu-Gln-(Ser, Ala, Gly) motifs (Rut et al, 2020).  As SARS-CoV-2 MPro has no closely related homologues in humans, it represents an attractive drug target (Ullrich and Nitsche, 2020). In summary, the Mpro protease is a chymotrypsin-like cysteine protease, requires homodimerisation for proteolytic activity, cleaves the viral polyproteins in 11 distinct sites, exclusively after a glutamine residue. A fluorogenic substrate for Mpro assays is Ac-Abu-Tle-Leu-Gln-AMC.The protein amount or better its concentration in solution is quantified using either A280 (absorption at 280 nm with its specific absorption coefficient) or using the Bradford assay (uses the dye Coomassie Brilliant Blue). Both of these methods quantify the total amount of protein in a sample, no matter what the oligomerization state is.

<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. Trypsin can be inhibited by using trypsin inhibitor Alpha 1 Antitrypsin.</p>

Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.

Sucrose phosphorylase (sucrose glucosyltransferase, disaccharide glucosyltransferase, systemic name Sucrose:orthophosphate α-D-glucosytransferase; EC 2.4.1.7) is an enzyme that catalyzes the following reaction:sucrose + Pi ⇌ D-fructose + α-D-glucose-1-phosphateOne unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate under optimum conditions.

<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>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>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. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</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>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. The immobilized Lipase 070 has a temperature optimum at 45 °C and pH optimum between pH 5 and 8, and is covalently immobilized on a polymer resin. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</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>Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction:  Creatinine + H2O → N-Methylhydantoin + NH3  One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 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>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>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>

LacBuster™-S 1000 is an enzymatic product derived from microbial sources, specifically engineered for precision and efficiency. It is a beta-lactamase, which catalyzes the hydrolysis of the beta-lactam ring found in beta-lactam antibiotics such as penicillins and cephalosporins, rendering them inactive. The enzyme achieves this by breaking the amide bond within the beta-lactam ring, a critical structural component necessary for antibiotic activity.

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

<p>Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is an enzyme from the family of carbohydrolases acting specifically on α-1,6-glucosidic branch linkages in polysaccharides such as amylopectin or glycogen, but rarely hydrolyzes such bonds in pullulan. Isoamylase has been obtained from P. amyloderamosa and has a temperature optimum in the 30 – 40 °C range and pH optimum between pH 3 and 4.</p>

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.

<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>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.</p>

<p>Mannitol dehydrogenase (MDH, mannitol 2-dehydrogenase, EC 1.1.1.67) is an enzyme that catalyzes the following reaction:  D-mannitol + NAD+ ⇌ D-fructose + NADH + H+  One unit of mannitol dehydrogenase will generate 1.0 μmole of D-fructose per min in the presence of NAD+ at pH 8.6 and 40°C. NAD+ is available here and NADH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.</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>

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.

<p>Copper-containing enzyme that catalyzes the first step in the synthesis of melanin</p>

<p>Aldehyde dehydrogenase (EC 1.2.1.3) is the enzyme that catalyzes oxidation of aldehydes to carboxilic acids, using NAD+ as a cofactor in the following reaction: R-CHO + NAD+ + H2O → R-COOH + NADH + H+    One enzyme unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.</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>Cymit Quimica’s econoLuciferase™ (econoLuc Cymit Quimica Cat. No. L-8090) is a recombinant luciferase from the firefly Luciola lateralis that has been expressed as a luciferase-GFP fusion protein in E. coli.The luciferase enzyme has been optimized for increased thermo-stability by genetic modification to be stable for one hour at 37°C and up to two days at room temperature.Stabilized econoLuciferase™ thus overcomes the disadvantages and limitations of wild-type Luciferase, notably its short active life, outperforming enzyme from the Photinus pyralis firefly for both performance and stability.This optimized luciferase is the perfect enzyme for ATP detection assays in hygiene control, microbial tests using caged luciferins and it is the luciferase of choice for biochemical tests measuring ATP consumption and production in diverse enzymatic reactions.The product L-8090 is available on a large scale and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.</p>

<p>Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is the enzyme that cleaves α-1,6-glucosidic branch linkages in carbohydrates, namely amylopectin or glycogen.</p>

<p>Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension is an enzyme product, which is a purified protein extracted from the muscle tissue of rabbits. This enzyme plays a crucial role in glycolysis, specifically catalyzing the transphosphorylation of phosphoenolpyruvate (PEP) to pyruvate, generating ATP from ADP in the process. This step is a key regulatory point in the glycolytic pathway, which is essential for cellular energy production.</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>Elastase (EC 3.4. 21.36) is a serine protease that breaks down elastin fibers. One unit of Elastase release 1 nmol of p-nitrophenol per sec from BOC-L-alanine p-nitrophenyl ester at pH 6.5 and 37°C</p>

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 %).

<p>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 &gt;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 %).</p>

<p>Deoxyribonuclease II (DNase II, deoxyribonucleate 3'-nucleotidohydrolase, acid deoxyribonuclease, acid DNase, EC 3.1.22.1) is an endonuclease that cleaves DNA, yielding 3'-phosphate-terminated polynucleotides with a free hydroxyl group on position 5'. One unit of the DNase II will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at pH 4.6 and 25°C.</p>

L-Glutamate oxidase is a deaminating oxidoreductase that catalyzes the conversion of L-glutamate to ketoglutarate, ammonia and hydrogen peroxide. The enzyme has been shown to have significant potential for immobilization on an insoluble support such as silica gel, which would allow it to be used in assays requiring higher concentrations of substrate. This property is important for industrial applications such as biosensor development for clinical biochemistry and the food industry.

<p>A N-Acetyl Muramidase enzyme that cleaves N-acetylmuramyl-β(1-4)-N-acetylglucosamine linkage in peptidoglycan within the bacterial cell wall.</p>

<p>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 &gt; 6 months at 4-25°C can be guaranteed.<br>Key features are:</p>

Porcine Pancreatic 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. Please enquire for more information about Alpha Amylase, Porcine Pancreatic including the price, delivery time and more detailed product information at the technical inquiry form on this page

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.

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.

Cell wall enzyme

<p>Lipase 14 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 30-40°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 14 was shown to hydrolyze p-Nitrophenyl esters of butyrate (74 % activity compared to octanoate), octanoate (100 %), laurate (8 %), palmitate (5 %), stearate (4 %), arachidate (1 %) and behenate (0.6 %).</p>