Magic Red Cathepsin Flat Manual
Elevated cathepsin enzyme activity in serum or the extracellular matrix often signifies a number of gross pathological conditions. Cathepsin-mediated diseases include: Alzheimer’s; numerous types of cancer; autoimmune related diseases like arthritis; and the accelerated breakdown of bone structure seen with osteoporosis (1,2). Up-regulated cathepsin B and L activity has been linked to several types of cancer. These include cancer of the colon, pancreas, ovaries, breast, lung, and skin (melanoma) (3-6). Up-regulation of cathepsin K has been shown in lung tumors (8). Increased cathepsin K activity has also been linked to degenerative bone diseases including osteopetrosis and post-menopausal osteoporosis (1,7).
Cathepsins are usually characterized as members of the lysosomal cysteine protease (active site) family (9) and the cathepsin family name has been synomonous with lysosomal proteolytic enzymes (1). In actuality, the cathepsin family also contains members of the serine protease (cathepsin A,G) and aspartic protease (cathepsin D,E) families as well. These enzymes exist in their processed form as disulfide-linked heavy and light chain subunits with molecular weights ranging from 20-35 kDa (10). Cathepsin C is the noted exception, existing as an oligomeric enzyme with a MW 200 kDa (10). Initially synthesized as inactive zymogens, they are post-translationally processed into their active configurations after passing through the endoplasmic reticulum and subsequent incorporation into the acidic environment of the lysosomes (1,10).
Protease activity can be detected within whole living cells using ICT’s Magic Red™ substrate-based assay kits. Designated as the MR-Cathepsin product line, these kits allow researchers to quickly visualize intracellular cathepsin activity within their particular experimental cell line.
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