Enzymes in Recombinant Proteins

<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>

<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&amp;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>

<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>

<p>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>

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

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

<p>Glucosidases are enzymes belonging to the family of oxidoreductases. They catalyse the hydrolysis of starches to simple sugars. Glucosidase is widely used in the food, carbohydrate and biofuels industries. In recent years, its applicability has expanded to biotechnology for its potential application in bioenzymatic fuel cells.</p>

<p>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</p>

<p>selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity.  It has also been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.</p>

<p>Maltose phosphorylase (systematic name maltose:phosphate 1-beta-D-glucosyltransferase; EC 2.4.1.8) is an enzyme that catalyzes the following reaction:  maltose + Pi ⇌ D-glucose + beta-D-glucose 1-phosphate  One unit of maltose phosphorylase will produce 1.0 μmole of D-Glucose from maltose per minute at pH 7.0 and 30°C.</p>

<p>Glucose Dehydrogenase is an enzyme, which is typically derived from microbial sources such as bacteria and fungi. It functions by catalyzing the oxidation of glucose to gluconolactone, concurrently reducing a cofactor such as NAD⁺ or PQQ. This biochemical reaction is critical in various analytical applications due to its specificity and efficiency in glucose detection.Glucose Dehydrogenase is widely employed in the development of biosensors and diagnostic assays. Its primary application is in blood glucose monitoring devices, where its ability to accurately quantify glucose levels is crucial for managing diabetes. Additionally, it is utilized in research and development settings for biochemical assays that require precise glucose measurements. The enzyme's rapid and specific action on glucose molecules makes it an indispensable tool in both clinical and laboratory environments, contributing to advancements in biosensing technologies and metabolic studies.</p>

<p>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.</p>

<p>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.</p>

<p>Carboxypeptidase Y (EC 3.4.16.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues and it remains active in the presence of urea at low to moderate concentrations. One unit of the Carboxypeptidase Y will hydrolyze 1.0 μmole of a chromogenic peptide substrate, releasing C-terminal alanine and generating a light-absorbing product.</p>

<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>

<p>Myokinase (Adenylate kinase, EC 2.7.4.3) catalyzes interconversion between ATP, ADP and AMP by catalyzing the following reaction:ATP + AMP ⇌ 2 ADPOne unit of Myokinase will convert 1.0 µmol ATP and 1.0 µmol AMP to 2.0 µmol ADP per min at 25°C and pH 7.5.</p>

<p>E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg</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>

<p>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.</p>

<p>Acetylcholinesterase is an enzyme that breaks down acetylcholine</p>

<p>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 by 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>Superoxide dismutase is an enzyme that catalyzes the conversion of harmful superoxide into hydrogen peroxide and oxygen.</p>

<p>Invertase is an enzyme that catalyzes the hydrolysis of sucrose to glucose and fructose and can be found in plants and microorganisms</p>

<p>Lysozyme is a bacteriolytic enzyme, which is primarily derived from hen egg whites. It functions by hydrolyzing the β-1,4-glycosidic linkages in the peptidoglycan layer of bacterial cell walls, particularly in Gram-positive bacteria. This enzymatic activity results in the lysis and subsequent death of the bacterial cells, providing a potent antimicrobial effect.</p>

<p>Nucleoside phosphorylase (Purine nucleoside phosphorylase, PNP, PNPase, inosine phosphorylase, inosine-guanosine phosphorylase; EC 2.4.2.1) is an enzyme that catalyzes the following reaction:  purine nucleoside + Pi ⇌ purine + alpha-D-ribose 1-phosphate  One unit of nucleoside phosphorylase will phosphorylate 1.0 micromole of inosine to hypoxanthine and alpha-D-ribose 1-phosphate per min at pH 7.4 and 25°C.</p>

<p>α-Glucosidase 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>

<p>beta-Galactosidase (EC 3.2.1.23, shortly beta-Gal, also know as lactase) catalyses the hydrolysis of beta-d-galactoside in the presence of water to galactose and alcohol, or lactose into glucose and galactose. beta-Gal has a molecular weight of 540,000 and is composed of four identical subunits of MW 135,000, each with an independent active site. The enzyme has divalent metals as cofactors, with chelated Mg2+ ions required to maintain active site conformation. The molecule contains numerous sulfhydryl groups and is glycosylated.</p>

<p>Endo-β-1,4-Mannanase (other names Mannan endo-1,4-β-mannosidase, endo-β-1,4-mannase, β-mannanase B, β-1, 4-mannan 4-mannanohydrolase, endo-β-mannanase, β-D-mannanase, 1,4-β-D-mannan mannanohydrolase; EC 3.2.1.78) is an enzyme, catalyzing the hydrolysis of -1, 4-mannosidic linkages in mannans, glucomannans and galactomannans. One unit of Endo-β-1,4-Mannanase will release 1.0 µmole of mannose reducing-sugar per minute from a 3mg/ml mannan solution at pH 5.5 and 37degC.  Expressed in U/g.</p>

<p>DNase I (Deoxyribonuclease I, EC 3.1.21.1) is an endonuclease that cleaves DNA, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3'. On average it produces tetranucleotides. One unit of the DNase I will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at 25°C.</p>

<p>Lyticase is a lysing enzyme that is designed to lyse cells in a biological sample. It contains an optimized wild-type guanine nucleotide-binding protein and has been shown to have high enzyme activities. Lyticase has also been shown to be active against opportunistic fungal strains, such as Candida glabrata, by disrupting their cell membranes. Lyticase is classified as a signal peptide with nuclear DNA, which allows it to be used in wastewater treatment applications. The enzyme can also be used for the analysis of the Toll-like receptor (TLR) response of microbes due to its electrochemical impedance spectroscopy properties.</p>

<p>From pigeon breast muscle - Carnitine acetyltransferase (EC 2.3.1.7, also Carnitine O-acetyltransferase) is an enzyme that catalyzes the following chemical reaction: acetyl-CoA + carnitine ⇌ CoA + acetylcarnitine</p>

<p>A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyprotein</p>

<p>75u/mg - Glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) is an enzyme that catalyzes the following reaction:  glyceraldehyde 3-phosphate + NAD+ + Pi ⇌ glycerate 1,3-bisphosphate + NADH + H+  One unit of GAPDH will convert 1.0 μmole of glyceraldehyde 3-phosphate into glycerate 1,3-bisphosphate per minute at pH 8.5 and 37 °C in the presence of NAD+ and phosphate. NAD+ is available here.</p>

<p>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.</p>

<p>E. coli recombinant sialic acid aldolase (EC 4.1.3.3) from Pasteurella multocida.  One unit is defined as the amount of enzyme that catalyses the formation of 1 umol Neu5Ac from ManNAc and Pyruvate per minute at 37 ℃.Activity: 9U/mg</p>

<p>Thioredoxin reductase (TR, TrxR) (EC 1.8.1.9) is an enzyme that reduce thioredoxin using NADPH as a co-factor, and also contains FAD. One unit of thioredoxin reductase will raise increase light absorbance by 1.0 per minute at 412nm in the presence of thioredoxin and Ellman's reagent at pH 7.0 and 25 °C.</p>

<p>Phosphodiesterase II from bovine spleen is an enzyme derived from the spleen of cattle, which serves as a crucial biological catalyst for the hydrolysis of phosphodiester bonds in nucleotide sequences. This enzyme's mode of action involves cleaving the phosphodiester linkages within nucleic acids, facilitating the breakdown of these macromolecules into smaller nucleotide units.</p>

<p>Oxalate Oxidase, freeze-dried, is an enzymatic preparation that serves as a catalyst in biochemical reactions. This enzyme is derived from wheat, a common plant source, ensuring a naturally occurring origin. Its primary mode of action is the oxidation of oxalate into carbon dioxide and hydrogen peroxide. This biochemical activity is significant in various scientific applications, specifically in the breakdown of oxalate, which plays a crucial role in metabolic and environmental processes.</p>

<p>Glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the following reaction:  glycerol-3-phosphate + O2 ⇌ dihydroxyacetone phosphate + H2O2  One unit of Glycerol-3-phosphate oxidase will generate 1.0 μmole H2O2 per min at 37°C, under the presence of O2 and the optimal pH. If required, you can remove the build-up of hydrogen peroxide using catalase.</p>

<p>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.</p>

<p>Triose-phosphate isomerase (TPI, TIM; EC 5.3.1.1) is an enzyme that catalyzes the reversible isomerisation of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate:  DHAP ⇌ GADP  The reaction mechanism involves the formation of an enediol intermediate. One unit of Triose-phosphate isomerase will convert 1.0 μmole glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 and 25 °C.</p>

<p>Cholesterol oxidase (EC 1.1.3.6) is an enzyme that catalyzes the following reaction: cholesterol + O2 ⇌ cholest-4-en-3-one + H2O2One unit of cholesterol oxidase will convert 1.0 μmole of cholesterol into cholest-4-en-3-one per min at pH 7.5 and 25 °C. You can remove the build-up of hydrogen peroxide using catalase.</p>

<p>Glycerokinase (glycerol kinase, GP, ATP-glycerol 3-phosphotransferase; EC 2.7.1.30) is an enzyme that catalyzes the following reaction:  ATP + glycerol ⇌ ADP + glycerol 3-phosphate  One unit of Glycerokinase will convert 1.0 μmole of glycerol and ATP to glycerol 3-phosphate and ADP per min at pH 9.8 and 25 °C.</p>

<p>Poly(ethylene terephthalate) hydrolase is an enzyme involved in the breakdown of Polyethylene terephthalate which is present in many plastics Polyethylene terephthalate hydrolytic enzymes may be useful in biotechnology, for use in waste treatment, biocatalysis and biorecycling</p>

<p>Sarcosine oxidase (Monomeric sarcosine oxidase, MSOX, EC 1.5.3.1) is an enzyme that catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2 and formaldehyde in the following reaction:  CH3-NH2+-CH2-COO- + H2O + O2 → NH3+-CH2-COO- + H2O2 + CH2O or sarcosine + water + oxygen → glycine + hydrogen peroxyde + formaldehydeOne unit of Sarcosine oxidase will form 1.0 micromole of formaldehyde from sarcosine per minute at pH 8.3 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.</p>

<p>Expression system: E. coli&lt;br&gt;Length: 1-169, Partial&lt;br&gt;Activity: BLI</p>

<p>Expression system: HEK297 Cells&lt;br&gt;Length: 21-472, Full Length of Mature Protein&lt;br&gt;Activity: Not Tested</p>

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

<p>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</p>