		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.

Type	Isotype	Clone	Grade
Mab	IgG1,k	2Q524	Purified

Size		Storage	Shipping	Source	Host
100ug		-20°C	Blue Ice	Human	Mouse

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).