SERPINA1 Human, Active
Description
The SERPINA1 protein is purified by proprietary chromatographic techniques.
Product Specs
SERPINA1, a secreted serine protease inhibitor, plays a crucial role in regulating proteolytic activity by targeting enzymes like elastase, plasmin, and collagenase. Genetic defects in SERPINA1 can lead to conditions such as emphysema or liver disease. Notably, it demonstrates in vitro inhibition of human recombinant matriptase's catalytic domain. SERPINA1 levels surge as part of the acute phase response to inflammation and tissue damage. The interplay between SERPINA1 and SLC11A1 genes significantly influences the balance of elastase produced by leukocytes during phagocytosis.
Product Science Overview
AAT is a glycoprotein primarily produced in the liver and released into the bloodstream. It belongs to the serpin (serine protease inhibitor) superfamily, which includes proteins that inhibit proteases like trypsin, cathepsin G, thrombin, and tissue kallikrein . The primary function of AAT is to protect the lungs from neutrophil elastase, an enzyme that can degrade elastin and other structural proteins in the lung tissue .
Recombinant Alpha-1 Antitrypsin (rAAT) is produced using yeast or other expression systems to create a biologically active form of AAT that is structurally similar to the natural protein found in human blood . This recombinant form eliminates the risk of blood-borne infectious agents associated with plasma-derived AAT and allows for increased manufacturing efficiency .
Recombinant AAT is used in augmentation therapy for individuals with AATD. This therapy involves regular infusions of AAT to maintain protective levels in the blood and lungs, thereby reducing the risk of lung damage . Studies have shown that recombinant AAT can effectively prevent or attenuate elastase- and cigarette smoke-induced models of emphysema, providing greater protection against alveolar enlargement, lung dysfunction, and airway inflammation compared to plasma-derived AAT .
The production of recombinant AAT involves optimizing the expression system to maximize yield. For instance, using the methylotrophic yeast Pichia pastoris as a host has proven effective for producing and secreting biologically active AAT . Strategies such as optimizing codon usage, using effective signal sequences, and adjusting gene dosage have been employed to enhance the production levels of recombinant AAT .
