Technical Data
M2423-21
Matrix Metalloproteinase 7 (MMP-7, Matrilysin, Matrin, Pump1, Uterine Metalloproteinase, MPSL1)
Description:
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. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG1,k2Q524Purified
SizeStorageShippingSourceHost
100ug-20°CBlue IceHumanMouse
Concentration:
~2mg/ml
Immunogen:
Rectal carcinoma (SW837) cells.
Purity:
Purified.
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.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Imai, K. et al. (1995). Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precuror, interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 270: 6691–6697. 2. Ohuchi, E. et al. Clin Chima Acta 244:181-198 (1996).