Archaemetzincin-1 (AMZ1) Antibody

Background

AMZ1 is a member of the archaelysin family of zinc-dependent metallopeptidases, enzymes that cleave peptide bonds in a variety of substrates. AMZ1 is expressed in multiple tissues, where it functions in protein turnover, extracellular matrix remodeling, and cellular signaling. As a metallopeptidase, AMZ1 requires a zinc ion for catalytic activity, which stabilizes the enzyme's active site and facilitates hydrolysis of peptide bonds. AMZ1 is thought to participate in processes such as tissue development, wound healing, and immune responses by regulating extracellular matrix components and growth factors. Dysregulation of AMZ1 activity has been implicated in pathological processes such as fibrosis, inflammation, and tumor progression, where excessive matrix degradation or improper protease activity contributes to disease. AMZ1's ability to cleave a broad range of substrates highlights its importance in maintaining proteolytic balance, tissue homeostasis, and intercellular communication.