| Description | Product Descriptionalpha-D-mannosidase, p-nitrophenyl-alpha-mannosidase, alpha-D-mannopyranosidase, alpha mannosidase, exo-alpha-mannosidaseAlpha Mannosidase from Jack Bean cleaves α(1-2,3,6)-linked mannose.This enzyme is often used in conjunction with Core Alpha-(1-6) Mannosidase (E-AM02) if aProduct Descriptionalpha-D-mannosidase, p-nitrophenyl-alpha-mannosidase, alpha-D-mannopyranosidase, alpha mannosidase, exo-alpha-mannosidaseAlpha Mannosidase from Jack Bean cleaves α(1-2,3,6)-linked mannose.This enzyme is often used in conjunction with Core Alpha-(1-6) Mannosidase (E-AM02) if a noncleavable core α(1-6) mannose is present on the substrate.SpecifictyAll Alpha-(1-2,3,6)-linked mannosePurityEach lot of α(1-2,3,6) mannosidase is tested for contaminating substances by incubating the enzyme for 24 hours at 37°C with substrates indicated in the table below. No detectable activity is evident for any of these potential contaminants. The detection limit of this assay is 5 µU/mL (IUB).For the protease assay, 10 µg of denatured BSA is incubated for 24 hours with 2 µl of enzyme. Analysis of the BSA band after SDS-PAGE should show no evidence of degradation.Molecular weighttwo polypeptides of 64,000 and 44,000 daltonsSpecific Activity AssayOne unit of Alpha Mannosidase is defined as the amount of enzyme required to hydrolyze 1 µmole of p-nitrophenyl-alpha-p-mannoside to p-nitrophenol in 1 minute at pH 5.0 and 37˚C.ContentsAlpha-(1-2,3,6) Mannosidase in 150 mM sodium phosphate, 0.1 mM ZnCl2 pH 7.5. (pH 7.5).Included with 20 µL and 60 µL pack sizes:200 µl 5x Reaction Buffer 5.0 (250 mM sodium phosphate, pH 5.0).Suggested usage1. Add up to 1 nmol of oligosaccharide.2. Add deionized water to 15 µl.3. Add 4 µl 5x Reaction Buffer 5.0.4. Add 1 µL of enzyme5. Incubate ten minutes at 37˚C... Read More | A general purpose purified albumin, suitable for Westerns, enzyme systems and as a protein supplement | Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towardsArachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towards ?-D-Gal(1-3)-D-galNAc. It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose. PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa.● Ultrapure quality ● Strong anti-T activity ● Sugar specificity: ?-D-Gal-(1-3)-D-GalNAc ● Agglutinates rabbit erythrocytes at < 0.1 µg/ml after trypsin treatment of the cells ● Lyophilized powderProbe in histochemistry and immuno-histochemistry;Human erythrocyte/lymphocyte studies... Read More | Inquire | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |