Mouse MMP-3/Stromelysin-1 ELISA Kit PicoKine®

monoclonal antibody from rat|polyclonal antibody from goat

10 ng/tube

Matrix metalloproteinase-3 (MMP-3) also called stromelysin or transin, is a proteoglycanase closely related to collagenase (MMP1) with a wide range of substrate specificities. The complete primary structure for human MMP-3, which has 477 residues including a 17-residue signal peptide. MMP-3 and collagenase are 54% identical in sequence, suggesting a common origin for the evolution of the two proteinases. MMP-3 and collagenase expression are coordinately modulated in synovial fibroblast cultures. MMP-3 is a secreted metalloprotease produced predominantly by connective tissue cells. Together with other metalloproteases, it can synergistically degrade the major components of the extracellular matrix. It is capable of degrading proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen. MMP-3 genotype may be an important determinant of vascular remodeling and age-related arterial stiffening, with the heterozygote having the optimal balance between matrix accumulation and deposition.

Microplate Reader capable of reading absorbance at 450nm.
Incubator.
Automated plate washer (optional).
Pipettes and pipette tips capable of precisely dispensing 0.5 µl through 1 ml volumes of aqueous solutions.
Multichannel pipettes are recommended for large amount of samples.
Deionized or distilled water.
500ml graduated cylinders.
Test tubes for dilution.

Stromelysin-1

Secreted, extracellular space, extracellular matrix.

Belongs to the peptidase M10A family.