Recombinant Human SerpinA5/SERPINA5 Protein (His Tag)

Serpin A5 is a member of the human Serpin superfamily consists of at least 35 members. It is synthesized in the liver and has been detected in saliva, cerebral spinal fluid, amniotic fluid, tears and semen. As a potent inhibitor of the protein C anticoagulant pathway at the levels of both zymogen activation and enzyme inhibition, Serpin A5 additionally inhibits a variety of serine protease including thrombin, factor Xa, several kallekreins and acrosin. It plays a critical role in the processes of blood of blood coagulation and fertilization. Serpin A5 also inhibits urinary plasminogen activator (uPA), a mediator of tumor cell invasion, and regulates tumor growth and metastasis by inhibiting angiogenesis. Furthermore, recent studies have identified PCI as a potent and direct inhibitor of activated HGFA (hepatocyte growth factor activator), suggesting a novel function in the regulation of tissue repair and regeneration. Similar to Serpins C1 and D1, the thrombin inhibitory activity of serpinA5 is enhanced by heparin.

Acrosomal Serine Protease Inhibitor; PAI-3; PAI3; PCI; PLANH3; PROCI; Plasma Serine Protease Inhibitor; Plasminogen Activator Inhibitor 3; Protein C Inhibitor; SERPINA5; Serpin A5

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.