Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis (Bromme and Okamoto, 1995; Drake, F. et al 1996; Bossard et al, 1996).||Recombinant protein corresponding to aa115-329 from human Cathepsin K, expressed in E. coli. | |Molecular Weight: |~23.5kD (aa115-329)||Specific Activity:|~5000mU/mg (1U = 1umole/min/mg) as measured by Cathepsin K Activity Assay Kit||Inhibitors:|Leupeptin (IC50: 70 nM), E-64 (IC50: 5 nM), z-FF-FMK (35 nM)a and Cystine. Minimal effect shown by Pepstatin and PMSF (inhibitors of aspartyl and serine proteases respectively). No inhibition seen with EDTA or phenanthroline (classical inhibitors of metalloproteases).||Storage and Stability:|Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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