| Description | Specific for human alpha-Syuclein including phosphorylated Ser129. Clone No.: pSyn#64. | Preparation: Lyophilized
Achromopeptidase has a broad range of activity, lysing the cell walls of many pathological Gram positive organisms as well as a number of Gram-negative organisms. The product is available in both crude and pure forms.
Activity: purified 10,000 – 20,000 units/mg
Optimum pH: 7Preparation: Lyophilized
Achromopeptidase has a broad range of activity, lysing the cell walls of many pathological Gram positive organisms as well as a number of Gram-negative organisms. The product is available in both crude and pure forms.
Activity: purified 10,000 – 20,000 units/mg
Optimum pH: 7.5-8.5
Pkg: 100,000 units... Read More | Aldose Reductase acts as useful tool for the understanding of sorbitol’s quantitative effects on the body. Origin: Human muscle cell.
Specific activity: 1.4 - 1.6 units/mg.
Concentration: 1 units/mL
MW: approx. 36,000
Preparation: Enzyme is dissolved in 5 mM DTT, 50% glycerin and 50 mM Sodium Aldose Reductase acts as useful tool for the understanding of sorbitol’s quantitative effects on the body. Origin: Human muscle cell.
Specific activity: 1.4 - 1.6 units/mg.
Concentration: 1 units/mL
MW: approx. 36,000
Preparation: Enzyme is dissolved in 5 mM DTT, 50% glycerin and 50 mM Sodium phosphate buffer solution (pH 7.0).
Pkg: 0.4 un.... Read More | 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 |