Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. Interacts with DNAJC1. Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains. The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. N- and O-glycosylated. Alpha-1-antichymotrypsin can bind DNA. Belongs to the serpin family. It is uncertain whether Met-1 or Met-4 is the initiator. Extended N-terminus. Extended N-terminus. Extended N-terminus. Alpha-1 antichymotrypsin entry