| Application notes
(see key) | Recommended dilutions
SDS-PAGE: Use at an assay dependent dilution.
WB: Use at an assay dependent dilution. Predicted molecular weight: 74 kDa.
Zymography: The Rat MMP-2 is active and is ready for enzymatic activity if diluted into a buffer of 20 mM Tris-HCl, pH 7.4, containing 150 mM NaCl, 10 mM CaCl2, and 0.1 mM ZnCl2. It will be most active at 37 degrees C but is still active at lower temperatures.
This peptide can be used with studies using ab38917.
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 zinc endopeptidases. 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.
MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.
This protein degrades denatured collagen (gelatin) and a range of extracellular matrix components in vivo. The protein was tested for activity in a zymogram (1 mg/mL gelatin in a 10% acrylamide gel). The smallest amount loaded was 1 ng. |
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