Enzymes dans les Protéines Recombinantes

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>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>

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.

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.

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.

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.

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.

An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteins

<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>

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>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>

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>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>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>Plasmin, human is a serin protease which present in the blood and is involved in the cleavage of cross-linked fibrin, a process known as fibrinolysis.One unit will produce one micromole of P-Nitroanilide from D-Val-Leu-Lys-P-Nitroanilide per minute at pH 7.5 at 37°C</p>

Lipoxidase, from glycine max (soybean)

<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 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>Aspartic acid proteinase is a type of proteolytic enzyme, which originates from various biological sources including humans, fungi, and plants. It is characterized by its action via two critical aspartic acid residues in the active site, which facilitate the hydrolysis of peptide bonds in proteins. This enzyme operates optimally in acidic environments, making it crucial in processes like digestion and protein processing within cellular compartments such as lysosomes.</p>

<p>Lipase from *Candida antarctica* is an enzyme-based biocatalyst, which is derived from the yeast *Candida antarctica*. This enzyme operates via a catalytic mechanism that involves the hydrolysis of ester bonds in lipid substrates, thereby facilitating the breakdown of fats into glycerol and free fatty acids. Its catalytic efficiency and stability in various conditions make it highly versatile for industrial applications.</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 ICE lipase has been immobilized on a hydrophobic carrier by a covalent linkage. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.

<p>Phosphorylase B is an enzymatic protein, specifically an isoform of glycogen phosphorylase, derived from rabbit muscle. This enzyme plays a critical role in glycogen metabolism by catalyzing the phosphorolytic cleavage of α(1→4) glycosidic bonds in glycogen, releasing glucose-1-phosphate. The rabbit muscle source provides a well-studied model due to its high enzyme activity and availability, facilitating in-depth biochemical and structural analysis.</p>

<p>Nitrile hydratase 23 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.</p>

Creatinase is an enzyme (EC 3.5.3.3) that catalyzes the conversion of creatine to sarcosine and urea.

Luciferase enzymes sourced from Vibrio fischeri

Enzyme involved in protein translation and catalyzes the aminoacylation reaction

Alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the following chemical reaction: a primary alcohol + O2 + H2O ⇌ an aldehyde + H2O2   One unit of alcohol oxidase will oxidize 1.0 µmole of methanol to formaldehyde per min at pH 7.5 and 25 °C.

<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>Nitrilase (nitrile aminohydrolase; EC 3.5.5.1) in an enzyme that catalyzes hydrolysis of nitriles to carboxilic acids and ammonia:  R-CN + 2 H2O → R-COO- + NH4+  One unit of nitrilase will yield 1.0 μmol of ammonia per minute under optimal reaction conditions using acrylonitrile as a substrate.</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 03 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.

<p>Lipoprotein lipase is a critical enzyme used to modulate lipid processing, primarily sourced from mammalian tissues. It functions by hydrolyzing triglycerides present in circulating chylomicrons and very low-density lipoproteins. This enzymatic process liberates free fatty acids, which can subsequently be utilized as energy by peripheral tissues or stored in adipose tissue. Lipoprotein lipase is pivotal in lipid metabolism, participating in maintaining homeostasis of plasma lipid levels.</p>

<p>Glucose-6-phosphate isomerase (GPI, phosphoglucose isomerase/phosphoglucoisomerase, PGI, phosphohexose isomerase, PHI; EC 5.3.1.9) is an enzyme that catalyses isomerisation between Glucose-6-phosphate and Fructose-6-phosphate:  G6P ⇌ F6P  One unit of GPI will convert 1.0 mmole of Fructose-6-phosphate to Glucose-6-phosphate per minute at pH 7.4 and 25 °C.</p>

<p>α-Mannosidase (α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase, α-D-mannosidase, systematic name α-D-mannoside mannohydrolase; EC 3.2.1.24) is an enzyme that cleaves α-mannose to produce glucose. One unit of α-Mannosidase will hydrolyze 1.0 µmole of chromogenic phosphate mimic p-nitrophenyl-α-p-mannoside to p-nitrophenol in 1 minute at pH 5.0 and 37°C.</p>

The secreted phospholipase A2-IIA (sPLA2-IIA, PLA2, systematic name phosphatidylcholine 2-acylhydrolase; EC 3.1.1.4) is an enzyme that catalyses the hydrolysis of glycerophospholipids at the sn2 position, yielding 1-acylglycerophosphocholine and a fatty acid. One unit of secreted phospholipase A2-IIA will hydrolyze 1.0 μmole of substrate per min under optimal conditions.

α-N-Acetylglucosaminidase (recombinant Human NAGLU Protein),  degrades heparan sulfate by hydrolysis of terminal GlcNAc resides in N-acetyl-alpha-D-glucosaminides of heparan sulfate.Activity is measured by its ability to hydrolyse 4-Nitrophenyl 2-acetamido-2-deoxy-a-D-glucopyranoside EN03208 or EM31027. The specific activity is >900 pmol/min/μg, as measured under the decribed conditions.

Formaldehyde dehydrogenase (EC 1.2.1.46) is an enzyme that catalyzes the following reaction: formaldehyde + NAD+ + H2O ⇌ formate + NADH + H+ One unit of formaldehyde dehydrogenase will convert 1.0 µmole of formaldehyde to formic acid per minute at pH 7.5 and 37°C in the presence of NAD+.NAD+ is available here.

<p>Serratiopeptidase (serratio peptidase, serratia peptidase, serrapeptidase, serratia E-15 protease, serralysin, serrapeptase; EC 3.4.24.40) is a proteolitic enzyme (proteinase) that is produced by Serratia marcescens.</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>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>

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.

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.

Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, ptyalin; 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 salivary Alpha Amylase is supplied as clear, colorless liquid solution at ≥2000U/mL, specific activity ≥200 U/mg protein. Store at -20°C on arrival.

<p>eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v).  This research grade eXrase has low endotoxin, max 0.25 EU/kU.eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings:  • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.</p>

eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v). This tech grade version is our most cost effective endonuclease for R&D applications. eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings:  • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.

<p>Glutathione Reductase, baker's yeast, is an enzyme derived from the yeast species *Saccharomyces cerevisiae*. This enzyme is sourced from baker's yeast, providing a renewable and consistent product for various biochemical applications. Its mode of action involves catalyzing the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), using NADPH as an electron donor. This reaction is crucial for maintaining the intracellular redox balance by regenerating GSH, the primary cellular antioxidant.</p>

<p>Expression system: Baculovirus&lt;br&gt;Length: 1-415, Full Length&lt;br&gt;Activity: Not Tested</p>

Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family.

Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the GST superfamily and Sigma family.

Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type

<p>Endoproteinase Glu-C (Glutamyl endopeptidase, V8 protease, GluV8, EC 3.4.21.19) is a protease that hydrolyzes peptide bonds at the carboxylic side of either exclusively Glu, or Glu and Asp residues, depending on the buffer conditions. One unit of endoproteinase Glu-C will generate 1.0 μmole of p-nitroaniline from Z-Phe-Leu-Glu-pNA peptide mimic substrate per minute at pH 7.8 and 25 °C. Z-Phe-Leu-Glu-pNA substrate is available here.molecular weight ~ 27000.</p>