| Description | Features Ultrapure qualityNon-specific blood group activitySugar specificity: Gal > GalNAcPhytohaemagglutininLyophilized powderProduct descriptionCrotalaria juncea lectin is isolated from Sunn hemp seeds and purified by affinity chromatography. The lectin has a molecular weight of 124 kDa and is Features Ultrapure qualityNon-specific blood group activitySugar specificity: Gal > GalNAcPhytohaemagglutininLyophilized powderProduct descriptionCrotalaria juncea lectin is isolated from Sunn hemp seeds and purified by affinity chromatography. The lectin has a molecular weight of 124 kDa and is composed of four identical polypeptide chains of 31 kDa. The lectin has non-specific blood group activity (1). It displays specificity toward ß-galactosides and interacts with serum glycoproteins, cytochrome b5 and virus surface glycoproteins such as BVDV, influenza and bovine diarrhea (1).Crotalaria juncea is supplied as a white to yellowish lyophilized powder. The purity of Crotalaria juncea lectin is determined by SDS- PAGE, which generates one single band at 31 kDa corresponding to the four identical polypeptide chains. The lectin is available in vials containing 50 mg or 10 mg powder. The product is to be used for laboratory work only.ApplicationsStudies of virus surface glycoproteinsPurifying bovine diarrhea virus when immobilized an agarose gel Directions for useThe lectin may be reconstituted with 2 ml of deionized water before use. Spin the vial gently until full dissolution. Aggregation is thought to occur in the presence of high concentrations of 2-mercaptoethanol. The solution may be reconstituted in this buffer to desired working concentration. In absence of lactose the lectin will polymerize and storage at pH 8.6–8.8 causes precipitation.Shipping and storageThe product is shipped at -20°C however for over-the-day transport it may be shipped at ambient temperature. The lyophilized powder is stable for more than three years from production date when stored below -20°C. After reconstitution with deionized water, the solution may be stored frozen in working aliquots for up to 12 months... Read More | Inquire | Inquire | Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work Purified pectinase is a multi-component preparation highly effective in depolymerizing plant pectins with varying degrees of esterification. The product contains substantial hemicellulase, cellulase, pectinesterase and xylanase activities which together with pectin lyase and polygalacturonase work synergistically to digest plant cell wall tissues. When used with Worthington purified cellulase, purified pectinase has been found to be highly successful for generating good yields of viable protoplasts in several plant systems, e.g., corn, soybean, red beet, sunflower, tomato and citrus. In general, a concentration range of 0.1% to 0.5% pectinase (with accompanying 0.5% to 1.5% cellulase) used at 24°C to 37°C for periods of 1 to 16 hours will yield good results... Read More | 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 |