| Description | CUEDC2 Human Pre-designed siRNA Set A contains three designed siRNAs for CUEDC2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CUEDC2 siRNA-1: 5 nmol (HPLC) CUEDC2 siRNA-2: 5 nmol (HPLC) CUEDC2 siRNA-3: 5 nmol (HPLC) siRNA Negative CUEDC2 Human Pre-designed siRNA Set A contains three designed siRNAs for CUEDC2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CUEDC2 siRNA-1: 5 nmol (HPLC) CUEDC2 siRNA-2: 5 nmol (HPLC) CUEDC2 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 | Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential Crude collagenase preparations contain several isoforms of two different collagenases, a sulfhydryl protease, clostripain, a trypsin-like enzyme, and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective at breaking down intercellular matrices, the essential part of tissue dissociation. One component of the complex is a hydrolytic enzyme which degrades the helical regions in native collagen preferentially at the Y-Gly bond in the sequence Pro-Y-Gly-Pro, where Y is most frequently a neutral amino acid. This cleavage yields products susceptible to further peptidase digestion. Crude collagenase is inhibited by metal chelating agents such as cysteine, EDTA or o-phenanthroline but not DFP. It is also inhibited by α2-macroglobulin, a large plasma glycoprotein. Ca2+ is required for enzyme activity. Particular enzymatic profiles of each collagenase have been correlated with the tissues from which the cells for study were obtained (or with the uses to which the cells are put) and as a result of the correlations several types of crude collagenases have been established by Aladdin: Types 1, 2, 3, and 4.This collagenase has been tested with cell lines to verify the product is not cytotoxic. Collagenase is typically used to digest the connective components in tissue samples to liberate individual cells. The concentration for cartilage dispersal is 1-2 mg/ml, but literature searches should be performed for species specific and/or tissue specific concentrations... 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 | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa precursor protein that is cleaved at a dibasic proteolytic site into a 40 kDa membrane-bound protein termed MSLN and a 31 kDa shed fragment called megakaryocyte-potentiating factor (MPF) that is released from the cell. Cleaved, human MSLN remains attached to the cell surface via a GPI linkage and shares 58% amino acid sequence identity with mouse and rat MSLN. In human, alternate splicing generates additional MSLN isoforms that have either an eight amino acid insertion following Ser408 or a substituted C‑terminal region with no GPI anchor. Mesothelin is normally expressed on mesothelial cells in the pleura, pericardium, and peritoneum as well as in the developing and postnatal pancreas. It is up‑regulated in mesotheliomas and a range of carcinomas and adenomas. Mesothelin promotes tumor cell proliferation, migration, anchorage-independent growth, and tumor progression. It is co‑expressed with the tumor antigen CA125/MUC16 on advanced ovarian adenocarcinomas and interacts with this molecule to support cell adhesion. A soluble form of Mesothelin is released from tumor cells into the serum or tissue effusions... Read More |