Enzymes dans les Protéines Recombinantes

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

E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt

Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor.

Possesses low quercetin 3-O-glucosyltransferase, 7-O-glucosyltransferase, 3'-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro.

Responsible for the biosynthesis of pyroglutamyl peptides.

N/A.

In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.

Involved in translation termination in response to the termination codons UAA, UAG and UGA.

NAD-GDH Protein, Clostridium difficile, Recombinant (His) is expressed in E. coli.

Toxic component of a type II toxin-antitoxin (TA) system.

PKM2 Protein, Mouse, Recombinant (E.

Thrombin-like snake venom serine protease that clots fibrinogen by releasing fibrinopeptide A from the alpha chain of fibrinogen (FGA), induces platelet

Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein.

GFER Protein, Rat, Recombinant (His & SUMO) is expressed in E.

HDAC3 Protein, Human, Recombinant (His & SUMO) is expressed in E.

HINT1 Protein, Rabbit, Recombinant (His & Myc) is expressed in HEK293 mammalian cells with N-10xHis and C-Myc tag.

Catalyzes the oxidation of methanol to yield formaldehyde.

Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.

Specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin.

mTOR Protein, Human, Recombinant (His & Myc) is expressed in E.

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

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>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>

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>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>

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

<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>

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

<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>

Expression system: E. coli<br>Length: 52-308, Partial<br>Activity: Not Tested

<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>

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

<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>

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>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>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>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>

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.

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.

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>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>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>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>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>

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>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>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>

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.