AnaSpec Introduces Improved MMP Detection Solutions

Matrix Metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components (1,2). These enzymes are responsible for connective tissue deterioration, bone remodeling, and damaged tissue repair. They are also involved in a number of diseases, such as tumor development and metastasis (3-6) as well as in rheumatoid arthritis (7,8).

EnzoLyte Plus™ MMP assay kits provide an innovative solution for researchers who need to identify the activity of a specific MMP in a complex biological sample containing multiple MMPs and other peptidases. EnzoLyte Plus™ MMP Assay Kits integrate the specificity of a monoclonal antibody with the sensitivity of a fluorescence peptide substrate, detecting the presence of a particular MMP in biological samples, including serum, plasma, tissue homogenate, cell lysate, and synovial fluid.

The enhanced selectivity is possible through the inclusion of a monoclonal anti human-MMP coated 96-well plate (12 x 8 black strips). The antibody specifically captures the proenzyme and active forms of an MMP from a mixed biological sample. The wells are washed and subsequent addition and cleavage of the FRET peptide gives a fluorimetric reading that reflects the proteolytic activity of the specifically captured MMP. AnaSpec’s unique 5-FAM/QXLTM 520 FRET peptides provide highly sensitive fluorescence readouts at an emission wavelength of 520 nm with a convenient excitation of 490 nm. Experimental data confirms that these kits can measure subnanogram quantities of specific human MMPs, with no cross-reaction to other MMPs.

AnaSpec currently offers the following MMP-specific assay kits:

EnzoLyte Plus™ 520 MMP-1 Assay Kit
EnzoLyte Plus™ 520 MMP-9 Assay Kit
EnzoLyte Plus™ 520 MMP-13 Assay Kit

For more information visit our website.

References

1. Woessner, JF. Jr. and CJ. Taplin, J. Biol. Chem. 263, 16918 (1988).
2. Woessner, JF. Jr., FASEB J. 5, 2145 (1991).
3. Matrisian, LM. et al., Proc. Natl. Acad. Sci. U.S.A 83, 9413 (1986).
4. Collier, IE. et al., J. Biol. Chem. 263, 6579 (1988).
5. Salo, T. et al. J. Biol. Chem. 258, 3058 (1983).
6. Salo, T. et al. J. Biol. Chem. 260, 8526 (1985).
7. Chin, JR.et al. J. Biol. Chem. 260, 12367 (1985).
8. Okada, Y.et al. J. Biol. Chem. 261, 14245 (1986).