Enzyme

Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°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 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).

Lipase 09 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 35-55°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 09 was shown to hydrolyze p-Nitrophenyl esters of acetate (18 % activity compared to octanoate), butyrate (80 %), octanoate (100 %) and capate (40 %).

Hexokinase (EC 2.7.1.1) in an enzyme that catalyses the following reaction:  Glucose + ATP → Glucose-6-phosphate + ADP  One unit of hexokinase will phosphorylate 1.0 µmole of glucose per min at pH 7.6 and 25 °C in the presence of ATP.  The product is a lyophilized powder, ≥30 units/mg protein.

Supplied as lyophilisate containing 1% w/w X-Shining™ Luciferase. The improved, thermostable X-Shining™ Luciferase is suitable for any luciferin-luciferase-based assay using D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins). Examples of its typical applications include ATP tests in hygiene monitoring, ATP tests in drug screenings and bacteria identification in microbial assays. The termostable luciferase X-Shining™ has been optimised by genetic engineering for strongly increased thermostability and storage stability. In temperature stress tests, the enzyme survives temperatures of 60°C for over an hour, whereas a wild type luciferase from firefly is inactivated after only a few minutes. The extraordinary stability makes it user-friendly and eliminates some of the main disadvantages and limitations of the commonly used wild type luciferase. X-Shining™ Luciferase is supplied as a lyophilisate (1% w/w X-Shining™ Luciferase) or as aqueous solution with glycerol (BX174908), and it may be stored for months at room temperature without significant loss of function. Find out more about our innovative X-Shining range here X-Shining | Innovation | Cymit Quimica Carbosynth.

Penase (Penicillinase) is an enzyme, which is a type of β-lactamase sourced from various bacterial strains capable of deactivating penicillin. It accomplishes this by targeting the β-lactam ring, a crucial structural component of penicillin antibiotics, and hydrolyzing it, thereby neutralizing the antibiotic effect. This enzymatic action is a defense mechanism employed by certain bacteria to survive in environments saturated with penicillin-based antibiotics.

Elastase is a proteolytic enzyme that breaks down elastin

CS2 hydrolase (Carbon disulfide hydrolase; E.C. 3.13.1.5) is an enzyme that catalyzes the following reaction:  CS2 + 2 H2O → CO2 + 2 H2S  thus converting carbon disulfide into hydrogen sulfide and carbon dioxide.

Lipase 08 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 20-60°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 08 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (60 %), laurate (7 %), palmitate (0.5 %), stearate (0.2 %), arachidate (0.1 %) and behenate (0.1 %).

Entorokinase (also known as enteropeptidase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of  Entorokinase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.

DNA ligase (ATP) is an enzyme (EC 6.5.1.1) that ligates DNA strands, repairing nicks in double-standed DNA and coupling blunt-ended or cohesive DNA fragments. It requires 3′ hydroxyl and 5′ phosphate nucleoside ends for ligation and ATP as a cofactor.

DNA polymerase is an essential enzymatic protein, derived from various organisms including bacteria, archaea, and eukaryotes, which plays a pivotal role in the replication and repair of DNA. This enzyme functions by adding nucleotides to the growing DNA strand in a template-dependent manner, ensuring the accurate duplication of the genetic material. It operates through a polymerization mechanism, where nucleotides are selected and incorporated complementary to the template strand, facilitating the elongation of the new DNA strand in the 5' to 3' direction.

Please enquire for more information about Horseradish Peroxidase 01, rekombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page

Expression system: HEK293 Cells
Length: 21-431, Full Length of Mature Protein
Activity: Enzyme activity

Expression System: E. coli
Length: 1-391, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 25-503, Full Length of Mature Protein
Activity: Not Tested

Protease that has a low substrate specificity.

Expression system: E. coli
Length: 18-308, Full Length of Mature Protein
Activity: Not Tested

RAB10 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.

Expression system: E. coli
Length: 83-418, Partial
Activity: Not Tested

RNF114 Protein, Human, Recombinant (GST) is expressed in E. coli.

Expression system: E. coli
Length: 32-756, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-260, Full Length
Activity: Enzyme activity

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc).

Expression system: E. coli
Length: 1-208, Full Length of Mature Protein of Isoform 2
Activity: Not Tested

Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).

Expression System: E. coli
Length: 1-180, Full Length
Activity: Not Tested

Expression System: E. coli
Length: 229-594, Partial
Activity: Not Tested

Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).

Expression System: E. coli
Length: 270-469, 27 kDa interstitial collagenase
Activity: Not Tested

Expression System: E. coli
Length: 1-585, Full Length
Activity: Not Tested

Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of

Expression System: E. coli
Length: 1-14, Full Length
Activity: Not Tested

Expression System: P. pastoris (Yeast)
Length: 1-225, Full Length
Activity: Not Tested

Expression System: E. coli
Length: 33-417, Partial
Activity: Not Tested

Expression System: E. coli
Length: 96-584, Partial
Activity: Not Tested

Expression System: E. coli
Length: 1-254, Full Length
Activity: Not Tested

Expression System: E. coli
Length: 21-305, Full Length of Mature Protein
Activity: Not Tested

TMPRSS2 Protein, Human, Recombinant (Avi & His & MBP), Biotinylated is expressed in E.

Expression System: E. coli
Length: 21-458, Full Length of Mature Protein
Activity: Not Tested

Expression System: E. coli
Length: 1-377, Full Length
Activity: Not Tested

The enzyme has great affinity for glucose and mannose.

Expression System: E. coli
Length: 5-171, Partial
Activity: Not Tested

Expression System: P. pastoris (Yeast)
Length: 1-199, Full Length
Activity: Not Tested

Expression System: E. coli
Length: 187-586, Extracellular Domain
Activity: Not Tested

PTGES3 Protein, Human, Recombinant (His) is expressed in Yeast.

PLOD3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with N-10xHis tag.

Fukutin Protein, Cynomolgus, Recombinant (His & Myc) is expressed in E.

Metalloprotease that cleaves substrates preferentially between Phe-Phe residues.