Enzymes in Recombinant Proteins

<p>Aspartate Aminotransferase (AST), Recombinant is a purified enzyme product utilized extensively in biochemical research and clinical diagnostics. Derived from a recombinant source, this enzyme mirrors the naturally occurring AST found in human tissues, ensuring consistency and reliability in experimental setups.</p>

<p>Ultra nuclease (EC 3.1.30.2) is an enzyme that digests DNA and RNA in any form: single- and double-stranded, linear, circular and supercoiled. The ultimate reaction product is 5'-monophosphate oligonucleatides that are mostly three, four and five bases long. Please enquire for more information about Ultra nuclease, liquid, recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Lipase 17 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8. 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 17 was shown to hydrolyze p-Nitrophenyl esters of butyrate (2 % activity compared to octanoate), octanoate (100 %), laurate (20 %), palmitate (3 %), stearate (1 %), arachidate (1 %) and behenate (1 %).</p>

<p>Copper-containing enzyme that catalyzes the first step in the synthesis of melanin</p>

<p>Lipase 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°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 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).</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>

<p>Cholesterol dehydrogenase (EC 1.1.1.840) is NADP+-dependant oxidoreductase, that catalyses the following reaction:cholesterol + NADP+ + H2O → cholest-4-en-3-one + NADPH + H+This is achieved by oxidizing alcohol hydroxy-group into ketone. One unit of cholesterol dehydrogenase will produce 1.0 μmole of cholest-4-en-3-one per minute at pH 8.5 and 25 °C.</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>

<p>Collagenase is an enzymes that is responsible for breaking peptide bonds in collagen</p>

<p>Pyruvate kinase (from Rabbit muscle), ammonium sulfate suspension is an enzyme product, which is a purified protein extracted from the muscle tissue of rabbits. This enzyme plays a crucial role in glycolysis, specifically catalyzing the transphosphorylation of phosphoenolpyruvate (PEP) to pyruvate, generating ATP from ADP in the process. This step is a key regulatory point in the glycolytic pathway, which is essential for cellular energy production.</p>

<p>Cymit Quimica’s econoLuciferase™ (econoLuc Cymit Quimica Cat. No. L-8090) is a recombinant luciferase from the firefly Luciola lateralis that has been expressed as a luciferase-GFP fusion protein in E. coli.The luciferase enzyme has been optimized for increased thermo-stability by genetic modification to be stable for one hour at 37°C and up to two days at room temperature.Stabilized econoLuciferase™ thus overcomes the disadvantages and limitations of wild-type Luciferase, notably its short active life, outperforming enzyme from the Photinus pyralis firefly for both performance and stability.This optimized luciferase is the perfect enzyme for ATP detection assays in hygiene control, microbial tests using caged luciferins and it is the luciferase of choice for biochemical tests measuring ATP consumption and production in diverse enzymatic reactions.The product L-8090 is available on a large scale and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.</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>

<p>Endopeptidase, powder, is a proteolytic enzyme, which is typically derived from microbial, plant, or animal sources, each imparting unique specificities. This enzyme functions by cleaving peptide bonds within polypeptide chains, rather than terminal bonds, thereby facilitating the breakdown of proteins into smaller, more manageable peptide fragments. The mode of action involves recognizing specific amino acid sequences within the substrate, leading to targeted bond hydrolysis.</p>

<p>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.</p>

<p>Neutral Endopeptidase is an enzymatic product in liquid form, classified as food grade, which is derived from microbial fermentation or animal sources. Its primary mode of action involves the hydrolysis of peptide bonds within proteins, resulting in the breakdown of these macromolecules into smaller peptides and amino acids. This process is facilitated through the enzyme's specificity for neutral pH environments, where it effectively cleaves internal bonds within a protein chain.</p>

<p>Endonuclease, liquid, food grade is a biochemical enzyme, which is derived from microbial or bovine sources, with precision in hydrolyzing phosphodiester bonds within nucleic acids. This endonuclease cleaves the internal bonds of DNA and RNA, enabling the breakdown of these molecules into smaller nucleotide fragments. Its catalytic action is particularly useful in the controlled degradation of nucleic acids without affecting other macromolecules in the substrate.</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>

<p>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.</p>

<p>Sialic acid aldolase - crystalline is a purified enzyme product, which is typically derived from microbial sources, such as certain bacteria, that have evolved to metabolize sialic acids. This enzyme catalyzes a reversible aldol reaction between sialic acid and pyruvate, facilitating the cleavage or formation of sialic acid from N-acetylmannosamine and pyruvate. By breaking the carbon-carbon bond in sialic acid, sialic acid aldolase plays a critical role in the degradation and biosynthesis pathways of sialic acid, which are key factors in numerous biological processes.</p>

<p>Hydrolytic enzyme; biocatalyst in production of beta-lactam antibiotics</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>

<p>Glucosyltransferase201-freeze dried is an enzymatic preparation that is primarily sourced from bacterial or plant organisms. It functions by catalyzing the transfer of glucose moieties from donor molecules, such as UDP-glucose, to specific acceptor molecules, thus forming glycosidic bonds. This mode of action is crucial in the biosynthesis and modification of polysaccharides and glycoconjugates.</p>

<p>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.</p>

<p>Glucosyltransferase206-freeze dried is an enzymatic preparation designed for specific biochemical applications. It is derived from microbial sources, where it is produced and purified through advanced biotechnological processes. The enzyme functions by catalyzing the transfer of glucosyl units from donor molecules to specific acceptors, thereby forming glycosidic bonds. This mode of action is crucial in various biosynthetic pathways, particularly in the production of polysaccharides and structural carbohydrates.</p>

<p>Glucosyltransferase210-freeze dried is an enzyme preparation that catalyzes the transfer of glucose molecules. Derived from specific microorganisms, it facilitates biochemical reactions by adding glucose residues to various substrates, thereby modifying their structure and function. The enzyme functions through the glucosylation process, which is essential in synthesizing different polysaccharides and glycoconjugates.</p>

<p>L-Leucine dehydrogenase (Leucine dehydrogenase, systematic name L-leucine:NAD+ oxidoreductase (deaminating); EC 1.4.1.9) is an enzyme that catalyzes the following reaction:  L-leucine + H2O + NAD+ ⇌ 4-methyl-2-oxopentanoate + NH3 + NADH + H+  One unit of L-Leucine dehydrogenase will convert 1.0 µmole of L‑leucine into 4-methyl-2-oxopentanoate per min at pH 10.5 and 37 °C in the presence of NAD+. The enzyme requires NAD+ as a cofactor, it is available here.</p>

<p>Glucosyltransferase205-freeze dried is an enzyme preparation that is commonly used in biochemical and molecular biology research. It is derived from microbial sources, often from bacteria or fungi that are known for producing extracellular enzymes. The primary mode of action of Glucosyltransferase205 involves catalyzing the transfer of glucose residues from donor molecules, such as UDP-glucose, to acceptor molecules, forming glycosidic bonds. This enzymatic activity is crucial in the biosynthesis of polysaccharides, which are essential components in various biological structures and processes.</p>

<p>20mg/ml aq. solution.  Proteinase K is used for the general digestion of proteins and removal of protein contamination in nucleic acids. Addition of Protease K also stabilizes nucleic acids but degrading any nucleases present. Proteinase K is active in wide range of pH range, in the presence of SDS, urea and Guanidinium chloride at low to moderate concentrations. Proteinase K is also known under names of protease K and endopeptidase K.</p>

<p>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.</p>

<p>Glucosyltransferase204-freeze dried is an enzyme preparation, derived from specific strains of Streptococcus bacteria, which plays a crucial role in catalyzing the transfer of glucosyl units from donor molecules to acceptor carbohydrates, predominantly in the formation of glucans. This enzymatic activity results in complex carbohydrate structures essential for various biological processes.</p>

<p>Glucosyltransferase211-freeze dried is an enzyme preparation which is derived from microbial fermentation. This enzyme functions by catalyzing the transfer of glucosyl groups from activated donor molecules to specific acceptor substrates. Its mechanism of action involves the formation of glycosidic bonds, facilitating the synthesis of various oligosaccharides and polysaccharides.</p>

<p>OXA-11 (β-Lactamase) is an enzyme of the β-lactamase class, which is primarily derived from Gram-negative bacteria. This enzyme is characterized by its ability to hydrolyze β-lactam antibiotics, rendering them ineffective by breaking the β-lactam ring, a crucial component of these antibiotics. OXA-11 is a notable member of the oxacillinase group within class D β-lactamases, known for its resistance to penicillins and cephalosporins.</p>

<p>SPM-1 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from certain Gram-negative bacteria, such as Pseudomonas aeruginosa. This enzyme is characterized by its ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, due to the presence of a zinc ion in its active site. The zinc ion plays a crucial role in the catalytic mechanism by facilitating the cleavage of the β-lactam ring, rendering the antibiotic ineffective against bacterial cell wall synthesis.</p>

<p>KPC-1 (β-Lactamase) is a specialized enzyme, which is produced by certain Gram-negative bacteria, notably Klebsiella pneumoniae. It functions by hydrolyzing the β-lactam ring found in a wide range of β-lactam antibiotics, such as penicillins and cephalosporins. This enzymatic action effectively neutralizes the antibiotic's antimicrobial properties, rendering the drugs ineffective against bacteria that produce KPC-1.</p>

<p>NMCA (β-Lactamase) is an enzyme, specifically acclaimed for its role in conferring antibiotic resistance. It is derived from bacterial sources, where it naturally occurs as part of the bacterial defense mechanism against β-lactam antibiotics. NMCA (β-Lactamase) functions by hydrolyzing the β-lactam ring present in these antibiotics, effectively rendering them inactive. This mode of action disrupts the antibiotic's ability to inhibit cell wall synthesis within bacteria, thereby permitting bacterial survival and proliferation.</p>

<p>Endoglycosidase H (systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96) is a highly specific enzyme, that cleaves asparagine-linked mannose rich oligosaccharides. One unit of Endoglycosidase H will remove &gt;95% of the carbohydrate from 10μg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10μl.The product EEH01.7 is available as a large-scale bulk supply of liquid enzyme solution and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.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)</p>

<p>A proteolytic enzyme; degrades protein contaminants in nucleic acid preparations</p>

<p>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.</p>

<p>VIM-15 (β-Lactamase) is an enzyme product, specifically a metallo-beta-lactamase, which is sourced from certain resistant bacterial strains. This enzyme functions by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective. The primary mode of action involves the coordination of zinc ions at its active site, enabling the breakdown of a broad spectrum of beta-lactam antibiotics including penicillins, cephalosporins, and carbapenems. This enzymatic activity significantly contributes to antibiotic resistance, posing a challenge in the treatment of bacterial infections. Its prevalence is noted in healthcare settings, where multidrug-resistant organisms are a concern. VIM-15 is of particular interest in clinical microbiology research and antimicrobial resistance studies, where understanding its structure and function can aid in the development of new inhibitors, potentially restoring the efficacy of beta-lactam antibiotics against resistant strains. Its characterization and study are critical for developing strategies to combat antibiotic-resistant infections effectively.</p>

<p>Sphingomyelinase (SMase, Sphingomyelin phosphodiesterase, systematic name sphingomyelin cholinephosphohydrolase; EC 3.1.4.12) is an enzyme that hydrolyses sphingomyelin into phosphocholine and ceramide. One unit of sphingomyelinase will hydrolyze 1.0 µmole of chromogenic substrate analogue per minute at pH 7.4 and 37 °C.</p>

<p>Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.</p>

<p>PARP12 Protein, Human, Recombinant (His &amp; Myc) is expressed in E. coli.</p>

<p>Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc.</p>

<p>TREX1 Protein, Mouse, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>Removes the N-terminal methionine from nascent proteins.</p>

<p>FTO Protein, Human, Recombinant (His &amp; Myc) is expressed in E. coli.</p>

<p>May have a protective function during conditions of oxidative stress.</p>

<p>Degradation of inorganic polyphosphates (polyP).</p>

<p>Thrombin-like snake venom serine protease.</p>

<p>Fukutin Protein, Cynomolgus, Recombinant (His &amp; Myc) is expressed in E.</p>

<p>ENR Protein, Mycobacterium tuberculosis, Recombinant (His) is expressed in E.</p>

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

<p>Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.</p>

<p>N/A.</p>

<p>Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate</p>

<p>Plays an important role in regulating cell division and growth by reversible phosphorylation signaling.</p>

<p>SARM1 Protein, Human, Recombinant (His &amp; KSI) is expressed in E.</p>

<p>Serine racemase/SRR Protein, Human, Recombinant (His &amp; SUMO) is expressed in E. coli.</p>

<p>Required for the control of apoptosis during postnatal growth.</p>

<p>Snake venom serine protease that may act in the hemostasis system of the prey.</p>

<p>Highly specific endopeptidase that hydrolyzes lysyl bonds including the Lys-Pro bond.</p>

<p>MASP1 Protein, Human, Recombinant (His &amp; SUMO) is expressed in E.</p>

<p>Catalyzes the ferrous insertion into protoporphyrin IX.</p>

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

<p>Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan</p>

<p>Catalyzes the deacylation of triacylglyceryl and cholesteryl ester core lipids of endocytosed low density lipoproteins to generate free fatty acids and</p>

<p>Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.</p>

<p>CYPOR Protein, Mouse, Recombinant (His) is expressed in E. coli.</p>

<p>Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis.</p>

<p>Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.</p>

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

<p>Expression System: E. coli&lt;br&gt;Length: 2-333, Partial&lt;br&gt;Activity: Not Tested</p>

<p>Expression System: E. coli&lt;br&gt;Length: 1-153, Full Length&lt;br&gt;Activity: Not Tested</p>

<p>Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.</p>

<p>Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.</p>

<p>Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis.</p>

<p>Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes.</p>

<p>Destroys radicals which are normally produced within the cells and which are toxic to biological systems.</p>

<p>PADI3 Protein, Human, Recombinant (His) is expressed in Yeast.</p>

<p>Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway.</p>

<p>Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan</p>

<p>This enzyme hydrolyzes cefotaxime, ceftazidime and other broad spectrum cephalosporins.</p>

<p>Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth</p>

<p>Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.</p>

<p>PYGB Protein, Human, Recombinant (GST) is expressed in E. coli.</p>

<p>Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin.</p>

<p>Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications.</p>

<p>Essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack.</p>

<p>Single-stranded DNA-dependent ATPase and 5' to 3' DNA helicase.</p>

<p>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</p>

<p>RAB10 Protein, Human, Recombinant (His &amp; Myc) is expressed in Baculovirus.</p>

<p>PTPRS Protein, Mus musculus, Recombinant (His &amp; Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag.</p>

<p>E3 ubiquitin-protein ligase that mediates the ubiquitination of phosphorylated BCL2L11.</p>

<p>GSK3B Protein, Human, Recombinant (E.</p>

<p>RIPK2 Protein, Human, Recombinant (His) is expressed in E.</p>

<p>PLA2G5 Protein, Rat, Recombinant (His &amp; SUMO) is expressed in E.</p>

<p>NirK Protein, Rhizobium sullae, Recombinant (His) is expressed in E.</p>

<p>Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides.</p>

<p>The enzyme has great affinity for glucose and mannose.</p>

<p>PTGES3 Protein, Human, Recombinant (His) is expressed in Yeast.</p>