Serpin Family A Member 1, Serpin Peptidase Inhibitor, Clade A,
SERPIN1's primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE).
Store at -70°C
inhibitor of proteases
serpin family A member 1
cool packs or dry ice
Mentioned in the data sheet
Research area interests
Diseases associated with SERPINA1 include Emphysema Due To Aat Deficiency and Hemorrhagic Disease Due To Alpha-1-Antitrypsin Pittsburgh Mutation. Among its related pathways are Platelet activation, signaling and aggregation and FOXA1 transcription factor network.
Purified from human serum.
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50mM phosphate buffer pH 6.5; 100mM NaCl, without BSA and Azide
Available target modification
Inhibitor of serine proteases, Member of Serpin Family
See the data sheet
For Research Use only.