Enzymes dans les Protéines Recombinantes

<p>Glutathione peroxidase (EC 1.11.1.9) is an enzyme that reduces peroxides to limit oxidative damage, by catalyzing the following reaction:  2 GSH + H2O2 → GS–SG + 2 H2O  One unit of glutathione peroxidase will catalyze the conversion of 1.0 µmole of H2O2 per minute at pH 7.0 and 25 °C in the presence of reduced glutathione. Reduced glutahione is available here.</p>

<p>Cytochrome C oxidase (originally assigned EC 1.9.3.1, now re-assigned EC 7.1.1.9) is an enzyme that catalyzes the following reaction: 4 Fe2+ – cytochrome c + 4 H+ + O2 → 4 Fe3+ – cytochrome c + 2 H2O</p>

<p>Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.</p>

<p>Protein phosphatase 2C is a key enzyme, which is a serine/threonine-specific phosphatase, derived from various organisms including humans, plants, and bacteria. This enzyme plays a pivotal role in cellular signaling by removing phosphate groups from serine and threonine residues on target proteins, a process known as dephosphorylation. This action is crucial for the regulation of diverse cellular functions, including stress responses, cell division, and apoptosis.</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 Lipase 02 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.</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 Lipase 01 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.</p>

<p>Oxalate Oxidase, freeze-dried, from Wheat is an enzyme preparation which is derived from wheat and functions through the oxidative degradation of oxalate. This enzyme catalyzes the conversion of oxalate into carbon dioxide and hydrogen peroxide, utilizing oxygen as a co-substrate in the process. The activity of Oxalate Oxidase is crucial in biological and biochemical applications where oxalate degradation is required.</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 CalB01 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteins</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 CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>One unit will hydrolyse 1.0μmol of 4-nitrophenyl phosphate per minute at 37°C and pH 4.8.  Substrate for enzyme analysis is the 4-nitrophenyl phosphate disodium hexahydrate (EN08508).</p>

<p>L-Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: L-Asparagine + H2O → L-Aspartate + NH4+   One unit will yield 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 and 37 °C.</p>

<p>Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: Asparagine + H2O → Aspartate + NH4+   Industrially, asparaginase is used to reduce the formation of acrylamide in starch-containing food ingredients and products during production processes. Asparaginase has a temperature optimum in the 30 – 50 °C range and pH optimum between pH 8 and 9. One unit will yield 1.0 μmole of ammonia from asparagine per min.</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. The Phospholipase D Kit contains 4 enzymes with a broad pH range for transphosphatidylation activity.</p>

<p>Deoxycytidine kinase (dCK, EC 2.7.1.74) is an enzyme that catalyzes the following reaction: dC + ATP → dCMP + ADP  It can also use UTP as a donor of the phosphate group, and it can phosphorylate other deoxyribonucleosides (e.g. dA, dG) as well as nucleoside analogues (like clofarabine). One unit of dCK will convert 1.0 µmole of dC and ATP to dCMP and ADP per minute at pH 7.5 and 37°C.</p>

<p>Cathepsin B is a lysosomal proteolytic enzyme of the cysteine protease family. It is present in all mammalian cells. It is essential for the intracellular protein turnover.  Cathepsin B may be a useful tool in Alzheimer′s research, as it may have a role in the natural defense against the disease.</p>

<p>Adenylate kinase 1 (EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction:  ATP + AMP ⇔ 2 ADP  One unit of Adenylate kinase 1 will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at optimum conditions.</p>

<p>Chloroperoxidase (also known as chloride peroxidase, systemic name chloride:hydrogen-peroxide oxidoreductase, EC 1.11.1.10) is an enzyme that catalyzes chlorination of organic compounds. Overall reaction is the following:R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O; reaction intermediate is hypochlorous acid (HOCl). One unit of chloroperoxidase will convert 1.0 μmole of substrate per minute.</p>

<p>Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) 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. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Human pancreatic Alpha Amylase is supplied as clear, colorless to light yellow liquid solution at ≥400U/mL, specific activity ≥100 U/mg protein.Store at 2-8 °C on arrival.</p>

<p>Lipoxidase is an enzyme, which is typically sourced from various plant tissues, animals, and some microorganisms. It functions by catalyzing the oxidation of polyunsaturated fatty acids in the presence of oxygen. This enzymatic action results in the formation of lipid hydroperoxides, which are key intermediates in various biochemical pathways, including those involved in cell signaling and the modulation of gene expression.</p>