| Description | IL1A Human Pre-designed siRNA Set A contains three designed siRNAs for IL1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components IL1A siRNA-1: 5 nmol (HPLC) IL1A siRNA-2: 5 nmol (HPLC) IL1A siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 IL1A Human Pre-designed siRNA Set A contains three designed siRNAs for IL1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components IL1A siRNA-1: 5 nmol (HPLC) IL1A siRNA-2: 5 nmol (HPLC) IL1A siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, Product DescriptionEndo F2 cleaves N-linked (asparagine-linked) biantennary oligosaccharides from glycoproteins. It also will cleave high mannose glycans but at a 40x reduced rate. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact.Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However, for optimal results, denaturation of the glycoprotein is recommended.Contents60 µl aliquot of enzyme (0.3 U) in 10 mM sodium acetate 25mM NaCl, pH 4.5Included with 20 µL and 60 µL pack sizes:5x Reaction Buffer – 250 mM sodium acetate, pH 4.5Molecular weight 32,000 daltonsSpecific Activity Defined as the amount of enzyme required to catalyze the release of N-linked oligosaccharides from 1 micromole of denatured porcine fibrinogen in 1 minute at 37°C, pH 5.5. Cleavage is monitored by SDS-PAGE (cleaved fibrinogen migrates faster).Formulation The enzyme is provided as a sterile-filtered solution in 10 mM sodium acetate, 25mM NaCl, pH 4.5Specificity Endo F2 cleaves Asparagine-linked biantennary and high mannose glycans (at a 40X reduced rate). It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide, generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. In contrast, PNGase F removes the oligosaccharide intact. Endoglycosidase F2 is less sensitive to protein conformation than PNGase F and is therefore more suitable for deglycosylation of native proteins. However for optimal results, denaturation of the glycoprotein is recommended.Quality & Purity Endo F2 is tested for contaminating protease as follows: 10 µg of denatured BSA is incubated at 37°C for 24 hours with 2 µl of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation. The production host strain has been extensively tested and does not produce any detectable glycosidases.Stability Several days exposure to ambient temperatures will not reduce activity. Stable at least 12 months when stored properly.Directions for use 1. Add up to 200 µg of glycoprotein to an Eppendorf tube. Adjust to 38 µl final volume with de-ionized water. 2. Add 10 µl 5x Reaction Buffer 4.5 3. Add 2.0 µl of Endo F2 to the reaction. Incubate 1 hour at 37°C. Monitor cleavage by SDS-PAGEThe production host strain has been extensively tested and does not produce any detectable glycosidases... Read More | The Leuconostoc GPDH exhibits dual coenzyme specificity, namely NAD and NADP (Olive and Levy, Biochem., 6, 730 730, 1967). When assayed under conditions that are optimal for the particular coenzyme, the ratio of observed catalytic activity is NAD/NADP = 1.8 | 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 | Protein:BSA-Free |