Matrix metalloproteinase-24 (MMP-24) is mainly expressed in the nervous system and also in the lungs, kidneys and liver. It is a 64kDa protein whose gene is localized on human chromosome 20.
Specificity
Reacts with native and reduced MMP-24. The antibody recognizes the pro-form of MMP-24 as well as activation/breakdown products. The cytoplasmic domain of MMP-24 is detached when MT-MMPs shed from themselves, thus this antibody should not detect this form of MMP-24.
Immunogen
synthetic peptide corresponding to the cytoplasmic domain of mouse matrix metalloproteinase-24 (membrane-type matrix metalloproteinase-5)
Biochem/physiol Actions
Matrix metalloproteinase-24 (MMP-24) is involved in the conversion of pro-matrix metalloproteinase-2 to its functional active form. It may be important for brain development and studies have shown that it is overexpressed in gastric cancer.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 50% glycerol and 15 mM sodium azide.
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During progression of gastric cancer (GC), degradation of the extracellular matrix is mediated by the matrix metalloproteases (MMPs) and their tissue inhibitors (TIMPs): changes in the expression of these have been related to unfavorable prognosis in GC. To analyze the
American journal of physiology. Renal physiology, 281(2), F309-F317 (2001-07-18)
Matrix metalloproteinases (MMPs) are a family of proteolytic enzymes that degrade the extracellular matrix (ECM). The membrane-type matrix metalloproteinases (MT-MMPs) are a new family of MMPs that differ from other MMPs in that they have a transmembrane domain that anchors
Membrane-type 5 matrix metalloproteinase (MT5-MMP) expression is ubiquitous in brain development while restricted to regions of neuroplasticity in adult. In the multipotent NT2 model of neurogenesis and differentiation, MT5-MMP is differentially expressed with significantly higher mRNA levels in the differentiated
A cDNA encoding a new member of the membrane-type (MT) matrix metalloproteinase (MMP) family has been identified and cloned from a human brain cDNA library. The isolated cDNA encodes a polypeptide of 645 amino acids that displays a similar domain
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