Enzymes in Recombinant Proteins

<p>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 &gt;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 %).</p>

<p>PAIRED PRODUCTS AVAILABLE:</p>

<p>Lipase 65 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 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 65 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (87 %), laurate (5 %), palmitate (0.2 %) and stearate (0.1 %).</p>

Cellulase, powder is an enzymatic product derived from microbial fermentation, specifically sourced from fungi or bacteria known for their cellulolytic activity. Cellulase acts by catalyzing the hydrolysis of cellulose, breaking it down into smaller polysaccharides and glucose. This decomposition occurs through synergistic action by three main components: endoglucanases, exoglucanases, and β-glucosidases, each targeting specific bonds in the cellulose structure, resulting in its complete breakdown.

<p>Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industries</p>

Lipase CR 02 is a high-purity enzyme preparation, which is derived from the microbial fermentation of selected fungal strains. With a mechanism involving the hydrolysis of ester bonds in lipids, Lipase CR 02 facilitates the conversion of triglycerides into glycerol and free fatty acids. This catalytic activity positions it as an essential tool in various biochemical and industrial applications.

<p>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.</p>

PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as a large-scale bulk supply of liquid enzyme solution. See our PNGase F available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution.Also available is our endoH enzymes (EEH01.3 - research quantities and EEH01.7 - large scale bulk supply).

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.

Xylanase is an enzymatic product, which is typically derived from microbial sources such as fungi or bacteria. Its primary function involves catalyzing the hydrolysis of xylan, a major hemicellulose component found in plant cell walls. Through breaking down xylan into xylose and other oligosaccharides, xylanase significantly modifies plant material structure.

Heat Labile Uracil-DNA Glycosylase, 500 units, is an enzyme designed for molecular biology applications, primarily derived from a recombinant bacterial source. This enzyme effectively removes uracil from DNA molecules at temperatures that preserve the integrity of the DNA. With its heat-labile properties, the enzyme can be inactivated at moderately elevated temperatures, making it ideal for processes that require precise control over enzyme activity.

Endoglycosidase H (Endo H) is a highly specific enzyme that cleaves N-linked oligosaccharides from glycoproteins, targeting high-mannose and certain hybrid-type N-glycans. It does not act on complex-type N-glycans, which are typically processed further in the Golgi apparatus. Due to its specificity, Endo H is widely used in research to study intracellular protein trafficking and post-translational modifications, particularly those occurring during glycoprotein maturation.This product is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solutionSee our EndoH (EEH01.7) available for large-scale bulk supply of liquid enzyme solution for the deglycosylation of proteins in manufacture.For removal of all N-linked carbohydrates from proteins see Cymit Quimica's PNGase F enzymes (PNG01.3 - vials for research and PNG01.7 - large-scale bulk supply)

Amidase is a hydrolase acting on carbon-nitrogen bonds in linear amides, and can be used in hydrolysis of amides to acids. Amidase 01 is of bacterial origin (P. aeruginosa) and has been produced in E.coli.

Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide.  Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs.

PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application. PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as vials for research applications with pre-defined quantities (>250 kU/vial) of liquid enzyme solution . See our large-scale bulk supply of PNGase F for the deglycosylation of proteins in manufacture.Also available is our endoH enzymes (EEH01.3 - vials for research and EEH01.7 - large scale bulk supply).

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-phosphateOne unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate under optimum conditions.

Cell wall enzyme

BspQI is a Type IIS restriction endonuclease which only cleave one strand when binding to a DNA sequence.

<p>Endopeptidase, liquid, food grade, broad spectrum is an enzymatic product used in the food industry. It is derived from microbial sources, specifically engineered strains capable of producing high yields of proteolytic enzymes. This endopeptidase functions by hydrolyzing peptide bonds within proteins, targeting internal sites to break down long protein chains into smaller peptides and amino acids.</p>

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

<p>Lipase, powder, food-grade, broad spectrum is an enzyme product, which is derived from microbial sources such as fungi and bacteria through a fermentation process. This enzyme operates by catalyzing the hydrolysis of fats into free fatty acids and glycerol, facilitating the breakdown of complex lipid molecules.</p>

<p>Phospholipase A2, liquid, food-grade, is an enzymatic product derived from natural sources, typically microbial or animal tissues, utilized in various lipid modification processes. This enzyme specifically targets phospholipids, catalyzing the hydrolysis of the sn-2 ester bond, which releases free fatty acids and lysophospholipids. Its precise and efficient mode of action allows for targeted alterations in the lipid structure, offering potential benefits in modifying texture, flavor, and stability of food products.</p>

<p>Lipase 15 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 25°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 15 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (13 %), laurate (1 %), palmitate (1 %), stearate (&lt;1 %), arachidate (&lt;1 %) and behenate (&lt;1 %).</p>

<p>A general purpose growth medium supplemented with LacBuster™ to effectively neutralize beta-lactam antibiotics. This product is suitable for the cultivation of a wide variety of microorganisms for environmental monitoring within the pharmaceutical industry and for high performance monitoring of your isolators and clean rooms during beta lactam manufacture</p>

<p>Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is an enzyme from the family of carbohydrolases acting specifically on α-1,6-glucosidic branch linkages in polysaccharides such as amylopectin or glycogen, but rarely hydrolyzes such bonds in pullulan. Isoamylase has been obtained from P. amyloderamosa and has a temperature optimum in the 30 – 40 °C range and pH optimum between pH 3 and 4.</p>

<p>Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.</p>

β-Glucosidase (β-D-glucosidase, systematic name β-D-glucoside glucohydrolase; EC 3.2.1.21) is an enzyme that catalyzes the release the terminal glucose monomers from cellulose and the other oligo- and poly saccharides with β-1,4-linked glucosyl residues. One Unit of β-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic p-nitrophenyl β-glucoside per minute under optimum conditions.

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

<p>Ribonuclease H from Escherichia Coli is the enzyme that breaks down RNA strand in RNA-DNA duplexes. It acts by cleaving the phosphodiester bonds of RNA and produces 3' hydroxyl and a 5' phosphate groups at the cleavage site. A common use of Ribonuclease H is to remove RNA template after reverse transcription reaction.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

Lipase 12 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7.5 and temp. optimum at >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 12 was shown to hydrolyze p-Nitrophenyl esters of butyrate (60 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (30 %), stearate (14 %), arachidate (0.2 %) and behenate (0.2 %).

<p>Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction:  Creatinine + H2O → N-Methylhydantoin + NH3  One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 and 37°C.</p>

<p>Phosphoenolpyruvate carboxylase is an enzyme, often found naturally in the cytosol of plant cells, which is derived primarily from various plant species. It plays a crucial role in the photosynthetic process, particularly in C4 and CAM plants. By catalyzing the irreversible carboxylation of phosphoenolpyruvate (PEP) to oxaloacetate, this enzyme facilitates the fixation of carbon dioxide, a vital step in the conversion of carbon dioxide into organic compounds during photosynthesis.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.</p>

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.

Expression system: E. coli<br>Length: 26-408, Partial<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-418, Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 2-501, Full Length of Mature Protein<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-203 (mutation), Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-205, Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-285, Full Length<br>Activity: Not Tested

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

Expression system: E. coli<br>Length: 1-593, Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-586, Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 98-356, Partial<br>Activity: Cell Activity

<p>Expression System: E. coli&lt;br&gt;Length: 1-430 (mutation), Full Length&lt;br&gt;Activity: Not Tested</p>

Expression system: E. coli<br>Length: 1-403, Full Length<br>Activity: Not Tested

PARP14 Protein, Human, Recombinant (His & Myc) is expressed in HEK293.

Expression system: E. coli<br>Length: 1-312, Full Length<br>Activity: Not Tested

Expression system: E. coli<br>Length: 1-669, Full Length<br>Activity: Not Tested