Clone: 1B4.
Background: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including Collagen, gelatin, Fibronectin, Laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-3, MMP-10 and MMP-11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.
Positive Control: Oesophageal and gastric tissues. Expressed at higher levels in tumor.
Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP3 protein and mouse myeloma Ag8563 cells.
Purification Method: Protein A/G Chromatography.
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide.
References: 1. Knauper, V., et al. (1996). Activation of human neutrophil procollagenase by stromelysin 2. Eur. J. Biochem. 235(1-2);187-191
2. Saus, J. et al. (1988). The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin. J. Biol. Chem. 263;6742-6745.
UniProt: P08254 (Human).
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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