Protease activity assay kits
for cancer research
Cancer pathogenesis is closely associated with the activity of proteases. Accordingly, testing protease inhibitors is routinely investigated as one of the current anti-cancer strategies.
Each protease has its own substrate specificity, but some members from a same protease family, like the matrix metalloproteinases, can cleave a same substrate, allowing for the development of highly specific of broader protease assays.
We constantly innovate to provide the best portfolio of quantitative protease assays, most being based on the FRET principle using proprietary substrates. As a world leader in FRET peptide technology we are proud to offer the same variety of long wavelength quencher and dye pairings used in our catalog peptides.
Our Sensolyte Assay Kits enable extensive detection of protease activity to be faster, easier and compatible with HTS.
FRET occurs between a peptide tagged to a donor and an acceptor when placed within 10-100Å of each other resulting in the donor’s excitation fluorescence to be quenched by the acceptor. Enzymatic hydrolysis of the peptide results in recovery of the donor fluorescence following spatial separation of the donor and acceptor upon energy transfer.
|Dye (donor)||Quencher (acceptor)||Donor Ex/Em|
|SensoLyte® 520||5-FAM or HiLyte™ Fluor 488||QXL®520||
These substrates do not require a quencher and contain a C-terminal dye that does not fluoresce until it is cleaved from the peptide (fluorescent form of dye is released).
|Dye (donor)||Donor Ex/Em|