| Description | HOXD9 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXD9 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXD9 siRNA-1: 5 nmol (HPLC) HOXD9 siRNA-2: 5 nmol (HPLC) HOXD9 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:HOXD9 Human Pre-designed siRNA Set A contains three designed siRNAs for HOXD9 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components HOXD9 siRNA-1: 5 nmol (HPLC) HOXD9 siRNA-2: 5 nmol (HPLC) HOXD9 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 | 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent moiety 4-methylumbelliferyl (4-MU). This 4-Methylumbelliferyl α-L-iduronide form is the free acid, which offers a considerable weight for weight advantage over the 4-MU iduronide salt in terms of its application dose.:For further studies, use α-L-iduronidase gene silencing:siRNA and shRNA:reagents and α-L-iduronidase gene editing:CRISPR:knockout and activation products... Read More | 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 | Inquire | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase... Read More |