Dispase II Neutral Protease
Dispase II Neutral Protease
Dispase II Neutral Protease is a gentle, neutral protease widely used for tissue dissociation and cell isolation. This enzyme specifically targets extracellular matrix components such as fibronectin and type IV collagen, enabling the separation of intact cells from tissue matrices without damaging cell membranes. Its mild proteolytic activity makes it ideal for preparing primary cell cultures and maintaining high cell viability and surface receptor integrity.
Unlike other proteases, Dispase II demonstrates selectivity by not cleaving laminin, type V collagen, serum albumin, or transferrin. This specificity helps preserve essential basement membrane components, minimizing cellular stress during tissue dissociation. The enzyme’s action on Leucine-Phenylalanine bonds underlies its precise substrate targeting and efficient matrix degradation while avoiding nonspecific protein digestion.
Dispase II activity is influenced by various metal ions—Ca²⁺, Mg²⁺, Mn²⁺, Fe²⁺, Fe³⁺, and Al³⁺ serve as activators, enhancing its catalytic function. Conversely, chelating agents such as EDTA and EGTA, as well as heavy metals like Hg²⁺, inhibit enzyme activity by interfering with metal ion binding. This controlled balance of activation and inhibition allows researchers to fine-tune enzymatic conditions for optimal tissue dissociation and cell recovery.
