Collagenases degrade native helical collagen fibrils.
- Plays an important role in connective tissue metabolism
- Produced by specific cells involved in repairs and remodeling processes
- Type II enzyme that contains greater clostripain activity
Collagenase is used for collagen structural and biosynthetic studies. For tissue dissociation most researchers employ either crude collagenase preparations or chromatographically purified collagenase combined with other enzymes such as elastase, trypsin, and/or papain. Collagenase from Clostridium histolyticum has been used in a study to investigate the survivability of collagen micronetworks in the presence of collagenase. Collagenase from Clostridium histolyticum has also been used in a study to investigate the degradation of collagen by the cariogenic bacteria, Streptococcus mutans.
Specific Activity: >125 u/mg solid
Key Applications: Release of cells from animal tissues
Application Areas: Cell Biology & Analysis
Product Type: Proteins, Enzymes & Peptides
Biochemical Category: Proteins, Enzymes & Peptides
Presentation: Brown Lyophilized Powder
Format: Lyophilized powder
pH: 7-9 for the A-a enzyme (optimum pH)
Specificity: Clostridial collagenase I or clostridiopeptidase A degrades the helical regions in native collagen preferentially at the Y-Gly bond in the sequence -Pro-Y-Gly-Pro- where Y is most frequently a neutral amino acid. This bond in synthetic peptide substrates may also be split.
Solubility: Soluble in water.
Storage & Handling: Store at +4°C. Store Desiccated.