Dispase II Enzyme
Dispase II Enzyme
Dispase II Enzyme is a mild, high-purity neutral protease widely recognized for its ability to gently separate cells from tissues without damaging their membranes. It hydrolyzes the N-terminal peptide bonds of non-polar amino acid residues, making it ideal for applications that require maintaining cell viability and integrity. Its gentle action ensures that cells remain intact and functional, even after detachment, making it a preferred choice for tissue dissociation and in vitro cell culture work.
This enzyme specifically cleaves fibronectin and type IV collagen, key components of the extracellular matrix, while leaving laminin, type V collagen, serum albumin, and transferrin unaffected. This selectivity allows Dispase II to effectively dissociate cells while preserving essential structural proteins that contribute to cell health. As a result, it is especially useful in preparing primary cells or subculturing sensitive cell lines where other enzymes might cause excessive membrane damage.
In addition to its tissue-separation capabilities, Dispase II helps prevent cell clumping in suspension cultures, ensuring more uniform cell populations. The enzyme’s activity is enhanced by divalent and trivalent cations such as Ca²⁺, Mg²⁺, and Fe³⁺, while chelating agents like EDTA and EGTA inhibit its function. With its gentle yet efficient proteolytic action, Dispase II offers researchers a reliable and cell-friendly solution for precise tissue dissociation and cell isolation.
