You searched for: Enzymes

Supplier: Rockland Immunochemical

All enzymes and related reagents are configured as an integrated system and have been thoroughly tested.

Supplier: MP Biomedicals

For typical assay, dissolve enzyme at a concentration of 1 mg/mL in 0.05 M TES with 0.36 mM calcium chloride, pH 7.5

Supplier: MP Biomedicals

Beta-glucuronidases are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates

Supplier: MP Biomedicals

Zymolyase-20T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells.

Supplier: Rockland Immunochemical

All enzymes and related reagents are configured as an integrated system and have been thoroughly tested.

Supplier: MilliporeSigma

β-Galactosidase, E. coli an inducible enzyme not found in eukaryotic cells that is used as a reporter gene.

Supplier: MP Biomedicals

Unit Definition: One unit is the amount of enzyme that oxidizes one micromole of bilirubin per minute at 37 °C, pH 8.4.

Supplier: Enzo Life Sciences

Enzyme regulation and kinetics, comparative studies of substrate or inhibitor specificities, cleavage of target proteins. Assay or digest conditions can vary widely, but concentrations for the MMP enzymes can range between 10 and 300nM, or higher. Reaction temperatures can be between 25 and 37°C, and reaction times can range from 10 min to overnight, again depending on application and substrate. A typical assay buffer is 50mM HEPES, pH 7.0, 10mM CaCl2, 0.05% Brij-35. For more information, contact Enzo Life Sciences Technical Support.

Supplier: AGILENT TECHNOLOGIES, INC (CSD)

The enzyme releases Alpha (2,3)-, Alpha (2,6)-, Alpha (2,8)-, and Alpha (2,9)-linked N-acetylneuraminic acid from oligosaccharides and glycoproteins. It is also capable of releasing N-glycolylneuraminic acid.

Supplier: QUALITY BIOLOGICAL, INC.

Trypsin is a proteolytic enzyme used to detach adherent cell from culture vessel surfaces. Typical use includes removing adherent cells from a culture surface. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture.

Supplier: MP Biomedicals

Bromelain is a glycoprotein which is a highly active thiol proteinase (non-specific cysteine protease), which splits glycine esters but not lysine esters; it is also a protein-digesting and milk-clotting enzyme. Substrates susceptible to bromelain include all of the common protein materials such as gelatin, casein, gluten, collagen, elastin, globulins and muscle fiber protein.

Supplier: MP Biomedicals

Glucose oxidase is an FAD-containing glycoprotein. The enzyme is specific for β-D-glucose. O can be replaced by hydrogen acceptors such as 2,6-dichlorophenol indophenol. Glucose oxidase from Aspergillus niger is a dimer consisting of 2 equal subunits with a molecular mass of 80 kDa each. Each subunit contains one flavin adenine dinulceotide moiety and one iron. The enzyme is a glycoprotein containing ~16% neutral sugar and 2% amino sugars. The enzyme also contains 3 cysteine residues and 8 potential sites for N-linked glycosylation. Glucose oxidase is capable of oxidizing D-aldohexoses, monodeoxy-D-glucoses, and methyl-D-glucoses at varying rates. Glucose oxidase does not require any activators, but it is inhibited by Ag+, Hg2+, Cu2+, phenylmercuric acetate, and p-chloromercuribenzoate. It is not inhibited by the nonmetallic SH reagents: N-ethylmaleimide, iodoacetate, and iodoacetamide.

Supplier: MP Biomedicals

Trypsin is a porcine pancreas-derived enzyme that is commonly used for the dissociation and disaggregation of anchorage-dependent mammalian cells and tissues. The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture.

Supplier: MP Biomedicals

Pyruvate kinase from rabbit muscle is a tetramer consisting of four equal subunits of molecular weight 57 kDa. Pyruvate kinase catalyzes the following reaction: ADP + Phosphoenolpyruvate → Pyruvate + ATP . Both Mg2+ and K+ are required metal cofactors for optimal activity. The enzyme is inhibited by Ca2+. It is a key enzyme in glycogen metabolism.

Supplier: MP Biomedicals

From Trichoderma viride This enzyme shows a very high filter paper decomposing activity, as well as, appreciable xylanase and hemicellulase activity

Supplier: MP Biomedicals

Collagenases degrade native helical collagen fibrils. The enzyme has an important role in connective tissue metabolism and is produced by specific cells involved in repairs and remodelling processes. It is a type II enzyme that contains greater clostripain activity. It is generally used for heart, bone, muscle, thyroid, cartilage, and liver cells. Ca2+ is required for its activation while metal chelating agents such as cysteine, EDTA or o-phenanthroline inhibits its activity.

Supplier: Corning

Dispase is a bacillus-derived neutral metalloprotease that is recommended for recovering cell cultured on Corning® Matrigel® Basement Membrane Matrix. Dispase will yield a single cell suspension far more gently and effectively than trypsin, collagenase, or other proteolytic enzymes; it will not harm cells harvested for sub cultivation or bioassays. In addition, Dispase may be used for tissue dissociation. Dispase cleaves fibronectin, collagen IV, and to a lesser extent collagen I, but is does not cleave collagen V or laminin.

Supplier: Enzo Life Sciences

Produced in E. coli. cDNA encodes residues identical to Asn120-His404 (C-terminus) at Genbank Accession No. M87507, except for an Asp381 to Glu change, introduced to stabilize the enzyme against autoproteolysis.

Supplier: Promega Corporation

IdeS Protease is an immunoglobulin-degrading enzyme from Streptococcus pyogenes (IdeS). IdeZ Protease is an immunoglobulin-degrading enzyme from Streptococcus equi subspecies zooepidemicus.

Supplier: G-Biosciences

Proteinase K (also protease K, endopeptidase K, peptidase K or Tritirachium alkaline phosphatase) (EC 3.4.21.64) is a non-specifc, broad spectrum serine protease that is isolated from the saprophytic fungus Tritirachium album.

Supplier: MP Biomedicals

Pepsin, an acid protease, contains a proteolytic enzyme. Pepsin contains the 'cathepsin' component which has milk curdling activity. It has a broad range of substrate activity and demonstrates an esterase acitivity. It generally attacks peptide bonds.

Supplier: MP Biomedicals

Ficin is a purified ficin preparation which is extracted from the latex of the fig tree Ficus glabrata. Ficin is classified as a thiol protease. Ficin hydrolyses the peptide bonds where the carbonyl group is from phenylalanine or tyrosine. When used in conjunction with other plants proteases, papain or bromelain, a synergistic effect may be observed. Immobilized Ficin was specifically designed for cleavage of mouse IgG1 into F(ab')2 or Fab fragments.The immobilization of ficin enhances stability against denaturation, heat and autolysis. Immobilization also eliminates any potential for antibody-enzyme adducts that cause continued sample digestion.

Supplier: MP Biomedicals

Deoxyribonuclease from beef pancreas, DNase I, was first crystallized by Kunitz. It is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding 5'-phosphate terminated polynucleotides with a free hydroxyl group on position 3'. The average chain of limit digest is a tetranucleotide. DNase I acts upon single chain DNA, and upon double-stranded DNA and chromatin. In the latter case, although histones restrict susceptibility to nuclease action, over a period of time nearly all chromatin DNA is acted upon. According to Mirsky and Silverman, this could result from the looseness of histone attachment to DNA. They found that lysine-rich histones more effectively block DNase access to DNA than arginine-rich histones. Billing and Bonner suggest that DNase attacks the histone-free strand of chromatin DNA. Schmidt, et. al.indicate that hydrolysis of the histone-free region of DNA strands accounts for the initial rapid action of the enzyme on chromatin. Bollum reports degradation of synthetic homopolymer complexes by DNase I. The intracellular functions of the enzyme are probably controlled by a DNase inhibitor, which according to Lazarides and Lindberg is actin.

Supplier: MP Biomedicals

Pectinase is a macerating enzyme comprised of pectintranseliminase, polygalacturonase, pectinesterase, xylanase, hemicellulases and cellulases.
Pectinase is used in plant protoplast preparation to digest cell wall prior to organelle isolation.
Pectinase causes random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
Store at +4 °C, desiccate.

Supplier: New England Biolabs (NEB)

Thermolabile Proteinase K (TLPK) is an engineered, subtilisin-related serine protease that will hydrolyze a broad variety of peptide bonds.

Supplier: TCI America

CAS Number: 9001-33-6

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Thermo Scientific Chemicals

Papain

Supplier: MP Biomedicals

Readily soluble in water.

Supplier: Thermo Scientific Chemicals

Bromelain (from Stem)