HIMEDIA Collagenase Type I

HIMEDIA Collagenase Type I

Description:

Collagenase is an enzyme derived from the fermentation of Clostridium histolyticum. Collagenases are endopeptidases that digest native collagen in triple helix region. Collagenases have specificity for the sequence R-Pro-(-X-Gly-Pro) where X is most often a neutral amino acid. Bacterial collagenases have a broader specificity than vertebrate collagenases. Bacterial collagenases can degrade both water insoluble native collagens and water-soluble denatured collagens. The extracellular matrix in animal tissue is a complex mixture of collagens and other extracellular matrix proteins like glycoproteins and protoeglycans. This matrix must be effectively broken down to isolate single cells, without alteration of cellular structures. Crude collagenase is a mixture of collagenases and other proteolytic enzymes. It contains a sulphydryl protease, clostripain, a trypsin-like enzyme and an aminopeptidase. This combination of collagenolytic and proteolytic activities is effective in breaking down intercellular matrices, the essential part of tissue dissociation. Activity: One Collagen Digestion unit liberates peptides from collagen equivalent in ninhydrin color to 1.0µmole of leucine in 5 hours at pH 7.4 at 37°C in the presence of calcium ions. One Clostripain unit hydrolyzes 1.0µmole of (N-Qbenzoyl-L-arginine ethyl ester (BAEE) per min at pH 7.6 at 25°C in the presence of dithiothreitol (DTT). One Tryptic unit is that enzyme activity which hydrolyzes 1.0µmole of (N-Q-benzoyl-L-arginine ethyl ester (BAEE) in one min at 25°C and pH 7.6. One protease unit hydrolyzes casein to produce color equivalent to 1.0µmole tyrosine per 5 hours at pH 7.5 at 37°C. Activators: Ca2+ is required for enzyme activity.

Specifications:

MSE Supplies offers a wide range of HIMEDIA Products for Cell Culture and Molecular Biology. Contact us for more information.