Enzyme

hCAII-IN-3 inhibits key hCA isoforms with Ki: hCA I (403.8 nM), hCA II (5.1 nM), hCA IX (10.2 nM), hCA XII (5.2 nM); shows anticancer potential.

Expression system: E. coli<br>Length: 1-169, Partial<br>Activity: BLI

Expression system: HEK297 Cells<br>Length: 21-472, Full Length of Mature Protein<br>Activity: Not Tested

Cyclophilin A Protein, Human, Recombinant (His) is expressed in E.

ACE2/ACEH Protein, Human, Recombinant (hFc), Biotinylated is expressed in HEK293 mammalian cells with hFc tag.

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

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

Carboxypeptidase B2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Genetic engineers have used glutathione S-transferase to create the GST gene fusion system.

Protein phosphatase 1G, also known as Protein phosphatase 1C, Protein phosphatase 2C isoform gamma, Protein phosphatase magnesium-dependent 1 gamma, PP2C-gamma

VEGFR3/FLT4 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.

Fructose-2,6-biphosphatase 3, also known as 6-phosphofructo-2-kinase or PFK2 or PFKFB3, is a potent activator of phosphofructokinase, which is a rate-limiting

Carbonic Anhydrase 9 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with His and Avi tag.

GUCY2C Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Endopeptidase, liquid, food grade is an enzymatic product that functions as a crucial component in the hydrolysis of protein substrates. This enzyme is typically derived from microbial sources, such as bacteria or fungi, and is cultivated under controlled fermentation processes to ensure high purity and activity levels. The primary mode of action of endopeptidases involves the cleavage of peptide bonds within protein molecules, effectively breaking down long protein chains into smaller peptides and amino acids.

Dextranase (alternative names dextran hydrolase, endo-dextranase, endodextranase, dextranase DL 2, α-D-1,6-glucan-6-glucanohydrolase, 1,6-α-D-glucan 6-glucanohydrolase, EC 3.2.1.11) is dextran-degrading enzyme that hydrolyzes the α(1→6) glycosidic linkage of dextran, cutting it into progressively shorter fragments, ultimaly producing isomaltose (a disaccharide) and glucose. One unit of dextranase will cleave dextrane to yield 1.0 μmole of isomaltose per min at pH 6.0 and 37 °C.

Lipase 30 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 5.5-8 and temp. optimum at >55°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 30 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (72 %), laurate (38 %), palmitate (7 %) and stearate (2 %).

A catalase product which neutralizes hydrogen peroxide at much higher concentrations (>10 %) compared to pyruvate, which is only capable of completely neutralizing hydrogen peroxide at the lowest concentration tested (2 %). Catalase (EC 1.11.1.6) catalyzes the following reaction:2H2O2 → 2H2O + O21 unit of catalase will decompose 1.0 μmole of H2O2 per min at pH 7.0 and 25 °C.

Lipase 14 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 30-40°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 14 was shown to hydrolyze p-Nitrophenyl esters of butyrate (74 % activity compared to octanoate), octanoate (100 %), laurate (8 %), palmitate (5 %), stearate (4 %), arachidate (1 %) and behenate (0.6 %).

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.

Lipase 16 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at >40°C. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 16 was shown to hydrolyze p-Nitrophenyl esters of butyrate (58 % activity compared to octanoate), octanoate (100 %), laurate (40 %), palmitate (27 %), stearate (13 %), arachidate (2 %) and behenate (0.2 %).

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.Spray dried version of EPLD840.6_R

Lipase Y 01 is an enzymatic catalyst, which is derived from microbial fermentation with a specific mode of action involving the hydrolysis of triglycerides into glycerol and free fatty acids. This enzyme operates by breaking ester bonds in fats, facilitating their breakdown and conversion into simpler molecules.

A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of > 6 months at 4-25°C can be guaranteed.
Key features are:

Freeze-dried powder with 3300 IU beta-lactamase I activity per vial against all relevant penicillins.  Our penase (penicillinase) posesses a specific substrate range solely against all relevant penicillins.

LacBuster® Settle Plates contain a general purpose growth medium (tryptone soya agar) supplemented with LacBuster®, a high-performing beta-lactamase to effectively neutralize beta-lactam antibiotics. The media plates are suitable for the cultivation of a wide variety of microorganisms in environmental monitoring within the pharmaceutical industry.

Pyruvate oxidase is a phosphorylating oxidoreductase which uses FAD as a cofactor to convert pyruvate into acetate and CO2. Pyruvate oxidase (PoxB) is used in metabolism studies in bacteria and in clinical assays for pyruvate, and requires thiamine pyrophosphate (TPP) and magnesium alongside FAD for optimum activity.

Aldehyde dehydrogenase (EC 1.2.1.3) is the enzyme that catalyzes oxidation of aldehydes to carboxilic acids, using NAD+ as a cofactor in the following reaction: R-CHO + NAD+ + H2O → R-COOH + NADH + H+    One enzyme unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.

Peroxidase 12 recombinantly expressed in P. pastoria comes in a freeze-dried formulation. It has its pH optimum at 5-8 and temp. optimum at 20-40°C. 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. Peroxidase 12 was shown to act on styrene, veratryl alcohol, vanillyl alcohol, n-methyl anthranilate and thioanisole.

Please enquire for more information about Sucrose phosphorylase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page

Pancreatin is an enzyme preparation, which is derived from the porcine pancreas. This product contains a mixture of several digestive enzymes, including amylase, lipase, and protease. It is typically obtained through the extraction and purification of these enzymes from the pancreas of pigs, providing a natural and effective source for enzymatic activity.

Please enquire for more information about Ribokinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page

Glucosyltransferase227-freeze dried is an enzyme-derived product, originating from microbial sources known for its role in catalyzing the transfer of glucose moieties from a donor molecule to specific acceptor molecules. The enzyme operates by facilitating covalent bond formation between glucose and target substrates, displaying specificity that can be exploited in various biochemical pathways.