Mouse Anti-Matrix Metalloproteinase 7 (MMP-7, Matrilysin, Matrin, Pump1, Uterine Metalloproteinase, MPSL1)
H-MMP-7 is a member of the Matrix metalloproteinase family of endopeptidases, containing the canonical HExxHxxGxxH motif as a zinc binding active site. MMP-7 and MMP-26 (Matrilysin-2) are the only MMPs discovered that completely lack a hemopexin “regulatory domain” or hinge region. Like the other MMPs, MMP-7 is secreted as a zymogen, then activated. The 28kD form is reduced to 18kD by enzymatic cleavage after the conserved “cysteine switch.” MMP-7 is not constitutively produced. It is produced on demand in specific tissues. MMP-7 substrate specificity is broad, most closely resembling the activity of MMP-3 (Stromelysin-1). When MMP-7 production is stimulated, native MMP inhibitors (TIMPs) usually follow to quench them.
Applications
Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications have not been tested.
Recommended Dilutions
Western Blot: 10ug/ml. Band at ~30kD Immunohistochemistry (Paraffin-embedded tissue sections): 4-20ug/ml Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Rectal carcinoma (SW837) cells
Form
Supplied as a liquid in PBS, pH 7.0, 2% BSA (protease free)
Specificity
Recognizes the precursor form of human MMP-7. Does not crossreact with the active form of human MMP-7 or human MMP-1, 2, 3, 8, 9 and 13.
