|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||53977 Da|
|Other Names||Stromelysin-1, SL-1, Matrix metalloproteinase-3, MMP-3, Transin-1, MMP3, STMY1|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human MMP-3 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP-3 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.|
|Cellular Location||Secreted, extracellular space, extracellular matrix|
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Provided below are standard protocols that you may find useful for product applications.
Effective inhibitors of matrix metalloproteinases (MMPs), a family of connective tissue-degrading enzymes, could be useful for the treatment of diseases such as cancer, multiple sclerosis, and arthritis (1). Matrix metalloproteinase-3 (MMP-3) is a protein involved in tumor invasion and metastasis. MMP3 (stromelysin) is a secreted metalloprotease with a wide range of substrate specificities. MMP3 is synthesized in a preproenzyme form with a calculated size of 54 kDa and a 17-amino acid long signal peptide. Data indicate that the expression and the possible involvement of secreted metalloproteases in tumorigenesis result from a specific interaction between the transforming factor and the target cell, which may vary in different species (2). In neural studies, matrix metalloproteinase-3 (MMP-3) was newly induced and activated in stressed dopamine cells, and the active form of MMP-3 (actMMP-3) was released into the medium. The released actMMP-3, as well as catalytically active recombinant MMP-3 (cMMP-3) led to microglial activation and superoxide generation in microglia and enhanced DA cell death. (3).
1. Wilhelm SM, et al. Proc Natl Acad Sci USA 84(19):6725-9, 1987.
2. Pavlovsky AG, et al. Protein Sci, 8(7):1455-62, 1999.
3. Kim YS, et al. FASEB J 21(1):179-87, 2007.
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