Z-LR-AMC Fluorogenic Peptide Substrate
R&D Systems, part of Bio-Techne | Catalog # ES008
Substrate for Cathepsin B, Cathepsin L, and Cathepsin V
Key Product Details
Conjugate
7-Amino-4-Methyl Coumarin
Applications
Bioactivity
Product Specifications
Source
Z-Leu-Arg-AMC. Z: N-carbobenzyloxy; 7-Amino-4-methylcoumarin.
Predicted Molecular Mass
578 Da
Activity
The peptide substrate contains a highly fluorescent
7-amino-4-methyl coumarin (AMC) group that is efficiently quenched by the amide
bond formed between its amino group and the carboxyl group of the Arg residue.
It can be used to measure the activities of peptidases that are capable of
cleaving this amide bond, causing an increase in fluorescence.
It is an excellent substrate for many cathespins. For example, it has been used to assay following recombinant human or mouse cathespins (rhCathespins or rmCathespins) followed by Catalog # in parentheses: rhCathepsin B (953-CY), rmCathepsin B (965-CY), rhCathepsin L (952-CY), and rhCathepsin V (1080-CY).
It is an excellent substrate for many cathespins. For example, it has been used to assay following recombinant human or mouse cathespins (rhCathespins or rmCathespins) followed by Catalog # in parentheses: rhCathepsin B (953-CY), rmCathepsin B (965-CY), rhCathepsin L (952-CY), and rhCathepsin V (1080-CY).
Formulation, Preparation and Storage
ES008
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage | Samples are stable for up to twelve months from date of receipt at -20° C to -70° C. The substrate can be aliquoted and stored -20° C to -70° C in a manual defrost freezer for six months. Avoid repeated freeze-thaw cycles. Protect from exposure to direct light. |
Background: Protease Substrates
Additional Protease Substrates Products
Product Documents for Z-LR-AMC Fluorogenic Peptide Substrate
Product Specific Notices for Z-LR-AMC Fluorogenic Peptide Substrate
For research use only
Loading...
Loading...
Loading...
Loading...
Loading...