- Enzymes
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Enzyme (4380)
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- Molecular Weight: 22.4 kDa
Endoproteinase Asp-N (MS grade) is a metalloprotease that can specifically cleave the N-terminal side of aspartyl and cysteic acid residues.
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Driselase, Basidiomycetes sp, a complex mixt. of wall-digesting enzymes, is a specific commercial fungal protoplasting enzyme preparation. Driselase can be used in combination with lyase to promote protoplast formation in fungi. Driselase is by far the most potent of the enzymes tested for polysaccharide digestion and greatly increases both tensile and indentation compliances, yet it does not induce wall creep, even after 6 h of digestion.
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Mucinase StcE is a zinc metalloproteinase belonging to the M66 family, which is secreted by enterohemorrhagic Escherichia coli via the type II general secretion pathway. Mucinase StcE specifically recognizes and cleaves the 'T*XT' motif in mucin-type glycoproteins with α-O-glycans (such as MUC2, Mucin 7, Glycoprotein 340, CD45, CD43, C1 Esterase Inhibitor (HY-P991629), etc.). By degrading the mucus layer to reduce its viscosity, inhibiting complement cascade activation, and localizing complement regulatory factors to the cell membrane, Mucinase StcE helps bacteria penetrate the mucosal barrier, adhere to host cells, and evade immune clearance. Mucinase StcE can serve as a mucin-specific proteolytic tool for research on mucinous carcinomas derived from the colon, esophagus, and salivary glands.
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Proteinase K (Protease K) (NGS grade) is a nonspecific serine protease that is useful for general digestion of proteins. Proteinase K (NGS grade) is active in the presence of SDS or urea and over a wide range of pH (4-12), salt concentrations, and temperatures. Proteinase K (NGS grade) can be use for promoting methods of viral nucleic acid extraction, and detection. This product is NGS grade, no Nickase residue, and nucleic acid residue ≤5 pg/mg.
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Collagenase (Type A, animal free) is a proteolytic enzyme targeting collagen, capable of releasing corneal endothelial cells (CECs) without damaging cell junctions.
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Aspartate aminotransferase (EC 2.6.1.1), porcine heart is a metabolic regulator with the highest activity in the heart, liver and skeletal muscle. Aspartate aminotransferase, porcine heart comprises two isozymes: the cytoplasmic form (AST1) and the mitochondrial form (AST2). By catalyzing reversible transamination reactions between oxaloacetate, L-glutamate and other substances, it is deeply involved in key physiological processes such as amino acid metabolism, the tricarboxylic acid cycle and neurotransmitter synthesis. Aspartate aminotransferase, porcine heart also provides substrate support for the synthesis of urea and purines/pyrimidines. Aspartate aminotransferase, porcine heart is a serum marker reflecting cardiac and hepatic injury, and its abnormal levels are also closely associated with myocardial infarction, cardiovascular diseases and various cancers.
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Formate dehydrogenase is a class of oxidoreductases widely distributed in bacteria, fungi, plants and animals. Formate dehydrogenase catalyzes the reversible conversion between formic acid and carbon dioxide, accompanied by redox reactions of the coenzyme NAD+/NADH or other electron carriers.
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Pyruvate Kinase, Microorganism (PK) is a glycolytic enzyme that catalyzes the conversion of phosphoenolpyruvate and ADP to pyruvate and ATP.
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PNGase F-Fast is a glycosidase that catalyzes the cleavage of internal glycosidic bonds in oligosaccharides. PNGase F-Fast removes almost all N-linked oligosaccharides from glycoproteins. PNGase F-Fast can release N-glycans from glycoproteins in the sugar analysis workflow. The cleavage site is: the glycosidic bond between the innermost N-acetylglucosamine and asparagine. PNGase F-Fast is an improved reagent that allows for rapid deglycosylation of antibodies and antibody fusions within minutes.
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Sortase A, S. aureus (SrtA), a transpeptidase enzyme is present in many Gram-positive bacteria and helps in the recruitment of the cell surface proteins. Sortase A, S. aureus plays an important part in ligation of various molecules on the cell surfaces.
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Formaldehyde dehydrogenase is a widely occuring enzyme that can catalyze S-hydroxymethylglutathione in the presence of NAD. Formaldehyde dehydrogenase detoxifies formaldehyde within cells through capturing and limiting it from reaching a toxic level. Formaldehyde dehydrogenase can be studied in research on M. tuberculosis.
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Micrococcal nuclease is a secreted nuclease from Staphylococcus aureus. It digests single-stranded and double-stranded DNA (ssDNA and dsDNA) as well as RNA, cleaves oligonucleotide linkers with T-T sites, and cuts neutrophil extracellular traps and biofilm extracellular DNA into mononucleotides and dinucleotides. Micrococcal nuclease stimulates the formation of Staphylococcus aureus biofilms and mediates immune evasion. It triggers on-demand release of antibiotics from hydrogel coatings, prolongs the formation of neutrophil extracellular traps, and promotes the dissemination and survival of MRSA during infection. Micrococcal nuclease is applicable to research and characterization related to Staphylococcus aureus infection.
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Recombinant myokinase, Rabbit muscle (Myokinase), is a phosphotransferase enzyme, is often used in biochemical studies. Recombinant myokinase, Rabbit muscle catalyzes the interconversion of adenosine phosphates. Recombinant myokinase, Rabbit muscle monitors phosphate nucleotide levels inside the cell, it plays an important role in cellular energy homeostasis.
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Dextranase, Trichoderma reesei belongs to glycoside hydrolase family 49. It catalyzes the hydrolysis of α-1,6-glycosidic linkages in dextran via a single-displacement reaction, ultimately releasing shorter isomaltooligosaccharides. Dextranase, Trichoderma reesei reduces the molecular size of dextran, inhibits the formation of insoluble dextran and dental plaque, and decreases the viscosity of dextran-contaminated sugar juice. Dextranase, Trichoderma reesei can be used in relevant research in fields such as chemical production, including beer manufacturing, feed additives, and toothpaste formulations.
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5α-reductase, Rat (Sprague-Dawley) Liver is an enzyme involved in steroid metabolism and participates in the androgen metabolic pathway. 5α-reductase, Rat (Sprague-Dawley) Liver catalyzes the conversion of testosterone to 5α-dihydrotestosterone (DHT). DHT plays important roles in the development of male sex organs, hair growth, prostate function, and other aspects.
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α-Glucosidase, bacillus stearothermophilus is a carbohydrase enzyme that catalyzes the release of α-glucose molecules. α-Glucosidase, bacillus stearothermophilus retains exoglycosidases, which hydrolyze α-glucosidic linkage at the nonreducing end of a substrate.
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- Molecular Weight: 290 kDa
Beta-glucuronidase (bovine liver) is a glycoside hydrolase that hydrolyzes β-glucuronic acid and sulfate esters in urine and other biological fluids, thereby releasing β-glucuronides. Beta-glucuronidase (bovine liver) cannot effectively hydrolyze Estriol glucuronide. Beta-glucuronidase (bovine liver) can be used in studies related to systemic gangliosidosis.
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