Procathepsin K from rat recombinant, expressed in E. coli, >=95% (SDS-PAGE)

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). Cathepsin K is produced as an inactive proenzyme (35.4 kDa) that is converted to its mature active form (23.5 kDa) by proteolytic cleavage of its 99-amino-acid propeptide domain. The in-vitro processing of procathepsin K to mature cathepsin K is autocatalytic.