Mouse Matrix Metalloproteinease-3 (Stromelysin-1) ELISA Kit

This Mouse Matrix Metalloproteinease-3 (Stromelysin-1) ELISA Kit from Innovative Research is intended for quantitative detection of mouse MMP-3 in cell culture supernates, serum and plasma (heparin). Strip well format. Reagents for up to 96 tests.

This mouse MMP-3 ELISA Kit was based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from rat specific for MMP-3 has been precoated onto 96-well plates. Standards(NSO, Y18-C477) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for MMP-3 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the mouse MMP-3 amount of sample captured in plate.

• Detection Target: Matrix Metalloproteinease-3 (Stromelysin-1)
• Uniprot ID: P28862)
• Reactivity: Mouse
• Cross-Reactivity: There is cross-reactivates with MMP-10 approximately 2% and no detectable cross-reactivity with other MMPs.
• Range: 156pg/ml-10000pg/ml
• Sensitivity: <10pg/ml
• Storage Conditions: Store at 4?C for 6 months, at -20?C for 12 months. Avoid multiple freeze-thaw cycles. (Shipped with wet ice)

Additional Information: The capture antibody is a monoclonal antibody from rat, the detection antibody is a biotinylated polyclonal antibody from goat. Expression system for standard: 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.; Immunogen sequence: 380