Matrix Metalloproteinase-3 (MMP-3) Human ELISA

Summary

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.1 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.2 The standard product used in this kit is recombinant human MMP-3, consisting of 460 amino acids with the molecular mass of 52KDa. The detected MMP-3 includes zymogen and active enzyme.

Research topic

Others

Assay format

Sandwich ELISA, Biotin-labelled antibody

Applications

Body fluids, Cell culture and/or animal studies, Plasma, Serum, Tissue lysates

Storage/Shipping

Store at 4°C for frequent use, at –20°C for infrequent use. Avoid multiple freeze-thaw cycles (Shipped with wet ice.)

Calibration Curve

Calibration range

156 pg/ml –10 000 pg/ml

Limit of detection

< 10 pg/ml

By research topic:

• Others

By molecule:

• Matrix Metalloproteinase-3 (MMP-3)