|
Specificity
|
The antibody binds to Gelatinase-A, but does not cross react with the other MMP family members (MMP-1, MMP-3, MMP-9, etc.).
We have a range of domain specific antibodies for this target. For a full list please see all MMP2 antibodies
|
|
Application notes
(see key)
|
Recommended dilutions WB: The recommended starting concentration for Western blots is 1/1000 when using colorimetric substrates such as BCIP/NBT, and 1/5000 for chemiluminescent substrates. Higher concentration of antibody may be needed for non-human samples. Detects a band of approximately 72 kDa (the pro-form) and 68 kDa (the active form) (Predicted molecular weight: 74 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 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.
|