Enzyme

<p>Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway.</p>

<p>Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA).</p>

<p>GSTA1 Protein, Rat, Recombinant (His &amp; SUMO) is expressed in E. coli.</p>

<p>Has no significant hemorrhagic activity, but inactivates serpins by limited proteolysis of their reactive-site loops.</p>

<p>Catalyzes the reversible oxidation of malate to oxaloacetate.</p>

<p>NME2 Protein, Human, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>Removes the formyl group from the N-terminal Met of newly synthesized proteins.</p>

<p>A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound</p>

<p>Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.</p>

<p>MBTPS1 Protein, Human, Recombinant (His &amp; SUMO) is expressed in E.</p>

<p>PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.</p>

<p>ZC3H12A Protein, Human, Recombinant (His) is expressed in E. coli.</p>

<p>Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan</p>

<p>Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.</p>

<p>Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes.</p>

<p>Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum.</p>

<p>Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion</p>

<p>Converts monoacylglycerides to free fatty acids and glycerol.</p>

<p>Cysteine proteinase with a strong preference for substrates with Lys in the P1 position.</p>

<p>Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.</p>

<p>Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and</p>

<p>Removes the formyl group from the N-terminal Met of newly synthesized proteins.</p>

<p>DNA repair enzyme that incises DNA at 8-oxoG residues.</p>

<p>Fructose 5-dehydrogenase [NADP(+)] Protein, Erwinia citreus, Recombinant (His &amp; KSI) is expressed in E. coli.</p>

<p>RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative</p>

<p>Essential virulence determinant.</p>

<p>N/A.</p>

<p>This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.</p>

<p>SIRT3 Protein, Mouse, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>HERC1 Protein, Human, Recombinant (His &amp; Myc) is expressed in E. coli.</p>

<p>CYP2C9 Protein, Human, Recombinant (His &amp; Myc) is expressed in E. coli.</p>

<p>Catalyzes the deacylation of triacylglyceryl and cholesteryl ester core lipids of endocytosed low density lipoproteins to generate free fatty acids and</p>

<p>Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.</p>

<p>N/A.</p>

<p>Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry.</p>

<p>Prothrombin Protein, Human, Recombinant (His &amp; SUMO) is expressed in E. coli.</p>

<p>Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription.</p>

<p>Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and</p>

<p>Cysteine protease that plays an important role in the inhibition of host innate immune response.</p>

<p>Probably mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4).</p>

<p>This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes.</p>

<p>WalK Protein, S.</p>

<p>Lys-gingipain W83 Protein, Porphyromonas gingivalis, Recombinant (His) is expressed in E.</p>

<p>Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-</p>

<p>Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity</p>

<p>Catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis.</p>

<p>EIF4A2 Protein, Human, Recombinant (GST) is expressed in E.</p>

<p>Functions as thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-</p>

<p>Presumably involved in the processing and regular turnover of intracellular proteins.</p>

<p>An NAD-dependent ADP-ribosyltransferase (ADPRT).</p>

<p>Modifies the functions of natural killer cells, monocytes and granulocytes.</p>

<p>Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.</p>

<p>Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis.</p>

<p>N/A.</p>

<p>Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway.</p>

<p>Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.</p>

<p>E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2.</p>

<p>Granzyme K/GZMK Protein, Mouse, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.</p>

<p>During the asexual blood stage, catalyzes the initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation; specifically cleaves between Phe-33</p>

<p>N/A.</p>

<p>Reelin Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 26.9 kDa and the accession number is P78509.</p>

<p>Removes the N-terminal methionine from nascent proteins.</p>

<p>NT5C1A Protein, Human, Recombinant (His) is expressed in Yeast.</p>

<p>Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-</p>

<p>Sortase A Protein, S.</p>

<p>PKM2 Protein, Rat, Recombinant (His &amp; Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag.</p>

<p>Releases the N-terminal proline from various substrates.</p>

<p>Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the</p>

<p>FDPS Protein, Human, Recombinant (His &amp; SUMO) is expressed in E.</p>

<p>FAM20C Protein, Mouse, Recombinant (His &amp; Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag.</p>

<p>Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose.</p>

<p>GLUL Protein, Cricetulus griseus, Recombinant (His) is expressed in E. coli.</p>

<p>Catalyzes the reverse reaction of octopine dehydrogenation.</p>

<p>FLP1 Protein, S.</p>

<p>RAN Protein, Human, Recombinant (GST) is expressed in E.</p>

<p>PRDX1 Protein, Cricetulus griseus, Recombinant (His) is expressed in yeast with N-6xHis tag.</p>

<p>PSMB8 Protein, Human, Recombinant (His &amp; Myc &amp; SUMO) is expressed in E. coli.</p>

<p>Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell</p>

<p>Major role in the synthesis of nucleoside triphosphates other than ATP.</p>

<p>GAPDH Protein, Cricetulus griseus, Recombinant (His) is expressed in E. coli.</p>

<p>Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and</p>

<p>MAT2A Protein, Human, Recombinant (His) is expressed in Yeast.</p>

<p>This protein degrades water-insoluble and water-soluble PHB to monomeric D(-)-3-hydroxybutyrate.</p>

<p>mTOR Protein, Human, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.</p>

<p>Phi29 DNA polymerase is a polymerase enzyme which has strong strand displacement activity, making it suitable for use in a range of displacement DNA amplification procedures</p>

<p>Protocatechuate 3,4-dioxygenase is a bacterial enzyme, which is sourced from Pseudomonas sp. This enzyme operates by catalyzing the cleavage of aromatic rings in protocatechuate, a derivative of catechol. Its mode of action involves the incorporation of oxygen into protocatechuate, resulting in the formation of beta-carboxy-cis,cis-muconate. This reaction is crucial for the microbial degradation of aromatic compounds, thereby playing a significant role in the biodegradation pathways of lignin-derived aromatic pollutants.</p>

<p>Chondroitinase ABC is a bacterial enzyme, which is derived from Proteus vulgaris with the ability to degrade glycosaminoglycans, specifically targeting chondroitin sulfate, dermatan sulfate, and hyaluronic acid. This enzyme's mode of action involves the enzymatic cleavage of β-1,4 linkages between N-acetylgalactosamine and glucuronic acid residues in chondroitin sulfate, resulting in the breakdown of these polyanionic molecules into disaccharides.</p>

<p>Alteplase is human plasminogen activator (EC 3.4.21.68, that cleaves plasminogen into enzymatically active form, plasmin), recombinantly expressed in CHO cells. Alteplase belongs to the group of thrombolytic agents, and it has shown to be effective in restoring blood flow by breaking down clots.</p>

<p>Expression system: E. coli&lt;br&gt;Length: 52-308, Partial&lt;br&gt;Activity: Not Tested</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT201 Glucosyltransferase, please see Table 1 that lists the available GTases with GT201 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT210 Glucosyltransferase, please see Table 1 that lists the available GTases with GT210 highlighted.Color: beigeForm: lyophilisateProtein content: 0.8 mg/mg The glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase Kit contains 2 recombinant peroxidases of bacterial and fungal origin with a temperature optimum in the 20-40 °C range and pH optimum between pH 5 and 8.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT211 Glucosyltransferase, please see Table 1 that lists the available GTases with GT211 highlighted.Color: beigeForm: lyophilisateProtein content 0.7 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT205 Glucosyltransferase, please see Table 1 that lists the available GTases with GT205 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 hr reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT204 Glucosyltransferase, please see Table 1 that lists the available GTases with GT204 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT227 Glucosyltransferase, please see Table 1 that lists the available GTases with GT227 highlighted.Color: beigeForm: lyophilisateProtein content: 0.8 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT206 Glucosyltransferase, please see Table 1 that lists the available GTases with GT206 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Glucosyltransferase (GTase) is the enzyme that transfers glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities. For the specificity of GT203 Glucosyltransferase, please see Table 1 that lists the available GTases with GT203 highlighted.Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.<br>Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.</p>

<p>Nitrile hydratase 22 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>

<p>LacBuster®-S 2000 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 2000 IU beta-lactamase II and 20000 IU beta-lactamase I activity per vial.</p>

<p>L-Glutamic dehydrogenase (NADP+ dependent, from proteus sp., EC 1.4.1.4)  is an enzyme that catalyzes the following reaction:  L-glutamate + H2O + NADP+ ⇌ 2-oxoglutarate + NH3 + NADPH + H+  One unit of L-Glutamic dehydrogenase will generate 1.0 μmole of 2-oxoglutarate from L-glutamate per min at pH 8.3, 30 °C and the presence of NADPH and ammonium. NADP+ is available here and NADPH is available here, depending on whether you require the reaction to proceed from left to right or from righ to left, respectively.</p>

<p>Kit of 10 unique, nitrile hydratases recombinantly expressed in E. coli for screening. 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. Please note, that the kit enzymes can also be supplied as whole cell biocatalysts in large scale.</p>

<p>Poly(ADP-ribose) glycohydrolase is an enzyme, which is derived from various organisms, including eukaryotic cells. It plays a crucial role in the regulation of poly(ADP-ribose) (PAR) metabolism. This enzyme functions by hydrolyzing the glycosidic bonds in poly(ADP-ribose) chains, thereby regulating the cellular levels of PAR by converting it back to ADP-ribose units.</p>

<p>Beta lactamase kit consisting of six different beta-lactamases with individual substrate specificity profiles against a broad range of beta-lactam antibiotics including penicilins, cephalosporins as well as carbapenems. The kit is especially designed for screening and finding the most well suited beta-lactamase for your specific process. Each vial contains at least 1000 IU beta I activity. Our beta-lactamases have been optimized for sterility testing and environmental monitoring in the manufacture and dosage formulation of beta-lactam antibiotics and for specific diagnostic purposes.Kit components:</p>

<p>Nitrile hydratase 19 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>

<p>Nitrile hydratase 01 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amidese, 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>

<p>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-phosphate  One unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate at pH 7.6 and 25 °C.</p>

<p>Enteropeptidase (historic name entorokinase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of enteropeptidase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.</p>

<p>One unit of aldolase (EC 4.1.2.13) will convert 1.0 µmol of Fructose-1,6-Diphosphate to Dihydroxyacetone phosphate and Glyceraldehyde-3-phosphate per min at 25 °C and pH 7.4. Lyophilized Powder.</p>

<p>Urease from Canavalia ensiformis (Jack bean urease, EC 3.5.1.5) is an enzyme that catalyses the following reaction:  (NH2)2CO + H2O → CO2 + 2 NH3  One unit of urease will yield 1.0 µmole of NH3 from urea per min at pH 7.0 and 25 °C.</p>

<p>Nitrile hydratase 14 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amidese, 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>

<p>Glutamic pyruvic transaminase (also Alanine transaminase, alanine aminotransferase; E.C. 2.6.1.2) is an enzyme that catalyzes the following reaction:  L-alanine + α-ketoglutarate ⇌ pyruvate + L-glutamate  One unit of Glutamic pyruvic transaminase will catalyze the conversion of 1.0 µmole per minute of L-alanine and α-ketoglutarate to L-glutamate and pyruvate, at 37°C and pH 7.4.</p>

<p>Nitrile hydratase 20 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>

<p>Nitrile hydratase 10 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>

<p>Ornithine decarboxylase (ODC1) is an enzyme which belongs to the Orn/Lys/Arg decarboxylase class-II family.</p>

<p>Carboxypeptidase A (EC 3.4.17.1) is an exopeptidase enzyme. It hydrolyzes peptide bonds of C-terminal residues with aliphatic or aromatic side-chains. One unit of Carboxypeptidase A will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 and 25 °C.</p>

<p>Heparinase I (heparin lyase I, heparin eliminase; EC 4.2.2.7) in an enzyme that specifically cleaves oligosaccharides to remove heparan sulfate residues. One unit will form 1.0 μmole of unsaturated uronic acid per minute at pH 7.5 and 25 °C.</p>

<p>Thioglucosidase (thioglucoside glucohydrolase, Myrosinase, sinigrinase, sinigrase; EC 3.2.1.147) is an enzyme that cleaves thio-linked glucosides:a thioglucoside + H2O ⇌ a sugar + a thiol (the thiol formed is usually unstable and undergoes spontaneous re-arrangement into a isothiocyanate through a loss of a sulfate group)One unit will produce 1.0 μmole glucose per min from sinigrin (a thio-linked glucoside) at pH 6.0 and 25 °C.</p>

<p>Neuraminidase (Exo-α-sialidase, sialidase, systematic name acetylneuraminyl hydrolase; EC 3.2.1.18) is an enzyme that catalyzes hydrolysis of glycosidic linkages of neuraminic acids. As it is exo-hydrolase, it hydrolyzes terminal N- or O- acylneuramic acid units, that are linked by α2,3-, α2,6-, and α2,8- glycosidic bonds. One unit of neuraminidase will hydrolyze 1 μmol N-acetyl-neuraminosyl-D-lactose under optimal conditions.</p>

<p>Glutaminase (glutaminase I, L-glutaminase, glutamine aminohydrolase; EC 3.5.1.2) is an enzyme that catalyzes the following reaction:  L-glutamine + H2O → L-glutamate + NH4+  One unit of glutaminase will convert 1.0 μmole of L-glutamine into L-glutamate per min at pH 4.9 and 37 °C.</p>

<p>D-Ribulose 1,5-diphosphate carboxylase, commonly known as RuBisCO, is an essential enzyme that catalyzes the first major step of carbon fixation, a process by which inorganic carbon from the atmosphere is converted into organic molecules. This enzyme is derived from spinach, a common model organism used in plant biology research due to its accessibility and well-characterized photosynthetic pathways.</p>

<p>Nitrile hydratase 17 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>

<p>Nitrile hydratase 05 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>

<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>