| Description | HM13 Human Pre-designed siRNA Set A contains three designed siRNAs for HM13 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HM13 siRNA-1: 5 nmol (HPLC) HM13 siRNA-2: 5 nmol (HPLC) HM13 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 HM13 Human Pre-designed siRNA Set A contains three designed siRNAs for HM13 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HM13 siRNA-1: 5 nmol (HPLC) HM13 siRNA-2: 5 nmol (HPLC) HM13 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 | Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.Laccase from Trametes versicolor has been used: to assess the use of four laccase-producing strains in waste water treatment in laccase assay in screening the lignolsSome of the enzymatic actions of laccase are associated with sporulation, detoxification, morphogenesis, melanin polymerization and it offers protection to spore coat. Laccase can catalyse a number of substrates including medicinal drugs and halogenated pesticides. It utilizes oxygen for its catalysis. For these reasons, it might be useful in the biological degradation of micropollutants in wastewater treatment. Laccase catalyzes the oxidation of phenol containing compounds, including lignin, through the reduction of oxygen to water. The presence of mediators will allow the oxidation of non-phenlic compounds as well. The primary function of laccase is to degrade lignin in fungi... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | Acid phosphatase is an esterase with broad activity at an optimal pH below 7.0. There are three isozymes, EI, EII, and EIII of similar molecular weight (55 kDa± 5 kDa). Their optimum pH's are 5.5, 4.5, and 4.0 respectively. Acid phosphatase activity was observed by Teller Aladdin Library Acid phosphatase is an esterase with broad activity at an optimal pH below 7.0. There are three isozymes, EI, EII, and EIII of similar molecular weight (55 kDa± 5 kDa). Their optimum pH's are 5.5, 4.5, and 4.0 respectively. Acid phosphatase activity was observed by Teller Aladdin Library Archives in 1954 in preparations of a wheat germ lipase described by Singer JBC, 174, 11, in 1948. Equivalent commercial preparations have been distributed labeled as lipase and acid phosphatase thus generating some confusion. Subsequent work has confirmed that the non-specific esterase activity of the wheat germ preparation may be measured both as lipase (triacetin as substrate) and phosphatase. The enzyme assay is based on the work of Brandenberger and Hanson (Helv. Chim. Acta, 36, 900, 1953) and Hofstee ( Arch. Biochem. Biophys., 51, 239, 1954).Acid phosphatase (APase) non-specifically catalyzes the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate. It is used to study the production, transport, and recycling of phosphate and the metabolic and energy transduction processes of the cell.Characteristics of Acid Phosphatase from Wheat Germ:Molecular weight: 55,000 ± 5,000 (Verjee 1969).Composition: Three isozymes of closely similar molecular weights have been reported by Verjee (1969): EI, EII, and EIII. See also Brouillard and Ouellet (1965).Optimal pH: EI - 5.5, EII - 4.5, and EIII - 4.0. (Verjee 1969).Specificity: The enzyme has a broad esterase activity. See Joyce and Grisolia (1960). It shows highest activity for pyrophosphate.Inhibitors: Fluoride, molybdate and orthophosphate (Verjee 1969)... Read More | Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine Purity>97% by SDS-PAGE and HPLC analyses.Additional sequence informationFunction N-terminal glycine. Full-length mature chain lacking the signal peptideFunctionHas chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity.Post-translationalN-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) are produced by proteolytic cleavage after secretion from peripheral blood monocytes... Read More |