| Description | This enzyme, isolated from Rhizoctonia solani is a lytic enzyme used to lyse cell walls and cell membranes for protoplast preparation. This multienzyme is also effective on filamentous fungi, algal cells, and plant cells.
Lytic Activity: min. 150,000 units/g Endo-ß-1,3-Glucanase activity: 2,000 This enzyme, isolated from Rhizoctonia solani is a lytic enzyme used to lyse cell walls and cell membranes for protoplast preparation. This multienzyme is also effective on filamentous fungi, algal cells, and plant cells.
Lytic Activity: min. 150,000 units/g Endo-ß-1,3-Glucanase activity: 2,000 units/g
Pkg: 1 g... Read More | Anti Iba-1 is specifically reactive to microglia and macrophages, and are appropriate for immuno-double staining of brain tissues and cell culture in combination with monoclonal antibody to GFAP, which specifically reactes to astrocytes. | 'Preparation: Lyophilized, salt-free
Specificity: In ammouniun carbonate buffer (pH 7.8 or ammonium acetate buffer (pH 4.0): Cleaves C-terminal peptide bonds of glutamic acid. In phosphate buffer (pH 7.8): Cleaves C-terminal peptide bonds of glutamic acid and aspartic acid.
Pkg: 50 µg | Apoptosis Inducer arrests tumor cells in late-S/G2 When methionine-dependent tumor cells in vitro are deprived of methionine they reversibly arrest in the late-S/G2 phase of the cell cycle. rMETase is an agent effective against all the major tumor types. Thus it is an excellent tool for the study ofApoptosis Inducer arrests tumor cells in late-S/G2 When methionine-dependent tumor cells in vitro are deprived of methionine they reversibly arrest in the late-S/G2 phase of the cell cycle. rMETase is an agent effective against all the major tumor types. Thus it is an excellent tool for the study of cell-cycle and anti-tumor agents. Pkg: 100 units... Read More | Lysyl Endopeptidase cleaves peptide bonds at the carboxy-terminal of both lysine residues and S-aminoethylcysteine residues, making it a valuable tool for analysis of peptide and protein primary structure and for enzymatic synthesis of Lys-X compounds. Also, it can retain complete activity after Lysyl Endopeptidase cleaves peptide bonds at the carboxy-terminal of both lysine residues and S-aminoethylcysteine residues, making it a valuable tool for analysis of peptide and protein primary structure and for enzymatic synthesis of Lys-X compounds. Also, it can retain complete activity after incubation in 4M urea or in 0.1% SDS solution.
This is package is designed for usage with mass spec. samples.
Pkg: 5 x 20ug... Read More |