Protease
Proteases, usually divided into serine proteases, cysteine proteases, metalloproteases and aspartic proteases, are widely found in animal organs, plant stems and leaves, fruits and microorganisms.
Protease are mainly used for:
• Catalyzing the hydrolysis of proteins and peptides
• Used in protein cleavage experimental procedures
Aminopeptidase N (rat) (APN/CD13) is a Zn2+-dependent membrane-bound exopeptidase that preferentially degrades proteins and peptides with N-terminal neutral amino acids. Aminopeptidase N (rat) is inhibited by angiotensin IV and participates in the regulation of angiotensin IV half-life in the rat striatum.
Chymase is a protein-digester enzyme found primarily in mast cells (MC), fibroblasts, and vascular endothelial cells. Chymase is released into the extracellular stroma in the context of inflammatory signals, tissue injury and cellular stress. Chymase is also involved in angiotensin II (Ang II) production, which is used in cardiovascular disease studies.
Pyroglutamate aminopeptidase I is a type of enzyme that cleaves the peptide bond of pyroglutamic acid linked to the N-terminal end of a protein, including some important anti-inflammatory proteins like immunoglobulin.
Protein disulfide isomerase is a prototypic thiol isomerase that catalyzes the formation and cleavage of thiol-disulfide bonds during protein folding in the endoplasmic reticulum (ER). Protein disulfide isomerase can be used for the study of cardiovascular diseases.
Sutilains is a proteolytic enzyme that dissolves necrotic tissue and hyaluronidase. Sutilains can be used as a topical debriding agent in burns.
Glutamic acid protease is a type of proteolytic enzyme containing glutamic acid residues, which mainly exists in fungi. Glutamic acid protease exerts its catalytic function through a glutamate-glutamine dyad.
