| Description | ALDOA Human Pre-designed siRNA Set A contains three designed siRNAs for ALDOA gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ALDOA siRNA-1: 5 nmol (HPLC) ALDOA siRNA-2: 5 nmol (HPLC) ALDOA siRNA-3: 5 nmol (HPLC) siRNA Negative Control:ALDOA Human Pre-designed siRNA Set A contains three designed siRNAs for ALDOA gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ALDOA siRNA-1: 5 nmol (HPLC) ALDOA siRNA-2: 5 nmol (HPLC) ALDOA 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 | Inquire | Inquire | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More | BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L,BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Unlike egg-white avidin, which has a net positive charge at neutral pH and contains about 7% carbohydrate, streptavidin has almost no net charge at neutral pH, does not contain carbohydrate, and exhibits lower non-specific background. Streptavidin conjugates are widely used together with a conjugate of biotin for specific detection of a variety of proteins, protein motifs, nucleic acids and other molecules. This FITC-streptavidin conjugate was prepared by highly purified Streptavidin and free FITC was removed. Streptavidin (FITC) is a useful second-step reagent for the indirect immunofluorescent staining of cells in combination with biotinylated primary antibodies for flow cytometric analysis. Excitation at 488nm light leads to a fluorescence emission maximum of 520 nm.Recommended Usage：Every lot of Streptavidin-FITC is tested by flow cytometry using biotinylated primary antibodies. From this testing it is recommended that between 0.02 and 0.25 µg of streptavidin be used per 106 cells in a 100 µl staining volume... Read More |