Collagenase is a protease that cleaves the bond between a neutral amino acid (X) and glycine in the sequence Pro-X-Gly-Pro, which is found with high frequency in collagen. Collagenase is unique among proteases in its ability to degrade the triple-helical native collagen fibrils commonly found in connective tissues such as skin, tendon, blood vessels, and bone. Collagenase disaggregation is suitable for the culture of human tumors, mouse kidney, human adult and fetal brain, and many other tissues including epithelium.
Collagenase is relatively gentle, dissociates well at physiological temperature and pH, and requires no mechanical agitation or special equipment.
Collagenase Type 1 is isolated from Clostridium histolyticum and packaged as a lyophilized, non-sterile powder for research use in cell or tissue dissociation, and organ perfusions. Collagenase Type 1 has the original balance of collagenase, caseinase, clostripain and tryptic activities.
