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Glutamate dehydrogenase (GDH, GLDH) ≥10 U/mg Substance (approx. 40 U/mg protein), lyophilized Unit definition One unit (U) is defined as the amount of enzyme that catalyses the reduction of one µmole of 2-oxoglutarate per min at pH 7.3 and 25 °C. Not a medical device / Not an IVD product
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Zymolyase ® , produced by a submerged culture of Oerskovia xanthineolytica, has strong lytic activity against living cell walls of various strains of yeast cells. Hence, it is frequently used in order to produce protoplasts or spheroplasts. The essential enzyme for the lytic activity of Zymolyase ® is β-1,3-glucan laminaripentaohydrolase. It hydrolyzes linear glucose polymers with β-1,3-linkages and releases specifically laminaripentaose as the main and minimum product unit. Directions for use Other confirmed side activities : β-1,3-glucanase, protease, mannanase; occasionally traces of other hydrolytic activities (e.g. amylase, phosphatase). Stability: At 30 °C 70 % of the lytic activity is lost after 3 months. Optimum temperature and pH: at pH 7,5 - 35 °C for lysis of viable yeast cells, at pH 6,5 - 45 °C for hydrolysis of yeast glucan. Specificity (lytic spectrum): Ashbya, Candida, Debaryomyces, Eremothecium, Endomyces, Hansenula, Hanseniaspora, Kloeckera, Kluyveromyces, Lipomyces, Metschnikowia, Pichia, Pullularia, Torulopsis, Saccharomyces, Saccharomycopsis, Saccharo mycodes, Schwanniomyces , etc. Stock solution: As stock solution, a 2 to 10 % (20 or 100 mg/ml) Zymolyase ® solution may be prepared, solubilizing the enzyme in water, 10 mM sodiumphosphate buffer (pH 7,4) or 50 mM Tris-Cl (pH 7,5), respectively, according to the buffer system to be used downstream and containing 5 % glucose and 50 % glycerol each. The Zymolyase ® tends to not dissolve completely. Do not heat for solubilization, but rather use the Zymolyase ® as suspension. The suspension may be stored in aliquots at -20 °C. Working solution: For use, Zymolyase is typically diluted immediately before application in the appropriate working buffer (e.g., 50 mM Tris-Cl, pH 7.5, 10 mM EDTA, 0.3% β-mercaptoethanol) to the desired final concentration. The optimal concentration depends on the enzyme type and protocol: For Zymolyase ® 100T: approx. 0.01–0.1 mg/ml; For Zymolyase ® 20T: approx. 0.05–0.2 mg/ml. Sterile filtration: Avoid using nitrocellulose filters when sterilizing - Zymolyase ® may be adsorbed to nitrocellulose membranes. Unit definition One unit of lytic activity is defined as the enzyme amount causing a decrease of 30 % in absorbance at 800 nm using 6 mg Brewer’s yeast as substrate in Phosphate buffer (pH 7,5) at 25 °C. Lytic activity varies depending on the particular yeast strain, the growth stage of the yeast, and cultural conditions. Zymolyase ® 100T ≥100 U/mg, lyophilized Zymolyase ® 100T is prepared by ammonium sulphate precipitatation, and is further purified by affinity chromatography.
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Invertase is an enzyme that catalyzes the hydrolysis of sucrose into the monosaccharides glucose and fructose. It is commonly derived from Saccharomyces cerevisiae (yeast) and occurs naturally in various organisms. Invertase is widely used in the food industry for the production of invert sugar, which is applied in sweets, jams, and beverages. It is also valuable in biotechnology and research, particularly in carbohydrate metabolism and enzyme kinetics studies. pH Optimum: 4.5–5.5 Temperature Optimum: 50–60 °C Invertase ≥50000 U/g, lyophilized Not a medical device / Not an IVD product
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Lysozyme ≥45 000 FIP U/mg, lyophilized Salt and albumin free lyophilised powder. Quality product for molecular biology. Ideal for lysis of bacteria for preparing DNA. Lysozyme preferentially hydrolyses the β-1,4-glycosidic bond between N-acetylmuraminic acid and N-acetylglucosamine. Muramic acid and acetylglucosamine are components of the proteoglycan cell wall of many microorganisms. The enzyme is mostly derived from chicken egg white and may efficiently be used for lysis of Gram+ bacteria. In genetic engineering, it is very often used during isolation of plasmid DNA or cellular RNA for the lysis of E. coli or eukaryotic cells. Unit definition 1 FIP-Unit equals the amount of enzyme which reduces the absorbance by 0.001 per min. at 450 nm, 25 °C, pH 7.00 using a suspension of FIP Micrococcus luteus as substrate (acc. to Pharmaceutical Enzymes 1997). 1 FIP-Unit resembles approximately 1 Shugar-Unit. Directions for use Working solution: 5-10 mg/ml (bacteria), 1-2 mg/ml (eukaryotic cells) Buffer: salt solution without detegents (0.1 M potassium phosphate buffer, 50 mM Tris buffer, 1x PBS, 1x TBS or similar) pH optimum: 6.0-7.0 Inhibitors: imidazole, indole, N-acetyl glucosamine Temperature optimum: 37 °C Stability: The lyophilisate is stable at +4 °C and -20 °C for several years. The stability of the solution at pH 4-5 is several weeks at +4 °C and several days at room temperature. Isoelectric point: approx. 11 Lysozyme solution should be frozen only once.
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Proteinase K (from Tritirachium album ) is a non-specific protease of the serine protease family. Proteinase K is used for the cleavage of proteins in nucleic acid preparations. It is mainly used in nucleic acid purification or for the removal of nucleases. Proteinase K is active under a wide range of reaction conditions, including elevated temperatures and presence of SDS. Directions for use Foreign activity: RNAse and DNAse not detectable Optimum temperature: +65 °C. Activity at +65 °C is ca. 12 x higher than at +25 °C. Over +65 °C, inactivation due to denaturation. Activators: Denaturating agents like SDS (0,5-1 %), urea. Inhibitors: Inhibition with Hg 2+ -ions, DFP, PMSF and phenol. Not inhibited by EDTA, sulfhydryl reagents and trypsin or chymotryps ininhibitors. Stability: pH 4.0-12.5. pH optimum: 8,0. Also stable even when denaturing agents, e.g. SDS and urea are present. Stabilisers: Ca 2+ -ions (1-5 mM) prevent autolysis. Proteinase K ≥30 mAnson U/mg, BioAnalysis Grade, lyophilized A non-specific endopeptidase with strong proteolytic activity for degrading proteins in biological samples. A quality product for molecular biology with a broad scope of application. Directions for use Working solution: 50 µg/ml Reaction buffer: 50 mM Tris-HCl; pH 7.5; 5 mM CaCl 2 ; 0.5 % SDS
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