Matrix metalloproteinases (MMPs)
MMPs belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components.1-2
The family currently includes more than 25 members that can be divided into collagenases (MMP-1, -8, and -13), gelatinases (MMP-2 and 9), stromelysins (MMP-3 and 10), matrilysins (MMP-7 and 26), and the membrane-type MMPs (MMP-14 to 17 and 24).
Collectively, MMPs cleave most, if not all, of the constituents of the extracellular matrix (ECM) and are involved in the breakdown and remodeling of many tissues and organs.
They preferentially cleave specific substrate sequences, but most often, one substrate can be cleaved by several MMP members.
AnaSpec is providing a comprehensive list of SensoLyte® assay kits to monitor the activity of MMPs and other adhesion-related proteases.
1. Woessner, J. et al. J. Biol. Chem. 263, 16918 (1988)
2. Woessner, J. FASEB J. 5, 2145 (1991)
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|