Lyophilized. Lyophilized from 2 mM sodium phosphate buffer, pH 6.5. Native cathepsin D from human liver. A major lysosomal aspartyl protease produced as a 52 kDa proenzyme. Overexpression of cathepsin D in human breast cancers is associated with higher risk of relapse and metastasis. Cathepsin D degrades extracellular matrix and releases growth factors bound to the matrix. Specific activity: ≥300 units/mg protein. One unit is defined as the amount of enzyme that will digest acid-denatured hemoglobin in 60 min, at 37°C, pH 3.3, releasing peptides soluble in 10% TCA, as measured by an increase in absorbance of 1.0 at 280 nm Purity: ≥90% by SDS-PAGE. Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. EC 3.4.23.5, CAS 9025-26-7. Merck Index: 14, 1905 Ref.: Berchem, G., et al. 2002. Oncogene 21, 5951. Barbi, G.P., et al. 1994. Oncology 51, 329. Krishnan, V., et al. 1994. J. Biol. Chem. 269, 15912. Touitou, I., et al. 1994. Eur. J. Cancer 30A, 390. Rijnboutt, S., et al. 1991. J. Biol. Chem. 266, 23586. Johnson, G.V., et al. 1991. J. Neurochem. 57, 1577. Erickson, A. 1989. J. Cell. Biochem. 40, 31. |