| Specificity | This antibody binds to the hinge region of MMP17. It can recognize native or reduced MMP17. The antibody does not cross react with the other MMP family members (MMP1, MMP2, MMP3, MMP9, etc.). We have a range of domain specific antibodies for this target. For a full list please see all MMP17 antibodies |
| Application notes
(see key) | Recommended dilutions
WB: 1/1000 when using colorimetric substrates such as BCIP/NBT - 1/5000 for chemiluminescent substrates. When used against the reduced protein identifies bands at 65 kDa and 63 kDa (the pro form and active form), as well as activation/breakdown products (predicted molecular weight: 67 kDa). Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user. |
| Relevance | The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.
MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported. |
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