Enzima

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.
Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.

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.
Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.

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.
Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.

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.
Not sure which GTase to choose? Consider our Glucosyltransferase kit, which contains all 8 Glucosyltransferases.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Citrate synthase (E.C. 2.3.3.1) is an enzyme that catalyzes the following reaction: acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SHOne unit of citrate synthase will form 1.0 μmole of citrate from acetyl-CoA and oxalacetate per min at pH 8.0 and 37 °C.Origin is porcine heart.Molecular weight ~ 49kDa (monomer) and  ~ 98kDa (dimer)

Specific activity: >500 units/mg-protein.Unit definition: One unit will polymerize 1.0 micro mole of ADP, releasing 1.0 micro mole of inorganic phosphate in 15 minutes at pH 9.1 at 37 °C.