serine protease inhibitor

Expression system: E. coli
Length: 1-142, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 722-847, Partial of Isoform l
Activity: Not Tested

Expression system: Baculovirus Insect Cells
Length: 25-405, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 23-402, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 22-418, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-418, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 24-80, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 17-86, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-416, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 21-414, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 43-417, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 28-491, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 25-413, Full Length of Mature Protein
Activity: Not Tested

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.

As protease inhibitors, serpins have an array of functions including regulating blood clotting, the complement pathway, extracellular matrix remodeling, and cell motility. Serpin G1 is a serine protease inhibitor protein. It is the largest member among the serpin class of proteins. Remarkably, Serpin G1 has a 2-domain structure, unlike most family members. The C-terminal serpin domain is similar to other serpins, and this part of Serpin G1 provides the inhibitory activity. The N-terminal domain is not essential for Serpin G1 to inhibit proteinases and has no similarity to other proteins. The main function of Serpin G1 is the inhibition of the complement system to prevent spontaneous activation. Serpin G1 is an acute phase protein and circulates in blood at levels of around 0.25g L, whose levels rise 2-fold during inflammation. Although named after its complement inhibitory activity, Serpin G1 also inhibits proteinases of the fibrinolytic, clotting, and kinin pathways. Most notably, Serpin G1 play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. It is also the most important physiological inhibitor of fXIIa, chymotrypsin and plasma kallikrein.

Serpin A1 is a prototype member of the Serpin superfamily of the serine protease inhibitors. As one of the most abundant proteinase inhibitors in the circulation, it is synthesized in hepatocytes, and to a lesser extent, in macrophages as well as intestinal epithelial cell lines and secreted as the abundant proteinase inhibitor in the circulation whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Point mutations in the native SerpinA1 variants result in Serpin A1 deficiency, and consequently lead to several clinical complications such as pulmonary emphysema, juvenile hepatitis, cirrhosis, and hepatocellular carcinoma. For example, the Z variants (Glu342 to Lys) forms intracellular inclusion bodies, is not secreted, and leads to a severe SerpinA1 deficiency. Accordingly, Serpin A1 deficiency in circulation is associated with emphysema or liver disease.

Plasminogen activator inhibitor-1 (serpin E1) is a serine protease inhibitor which belongs to the serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3 TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.

Expression system: HEK293 Cells
Length: 24-79, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-397, Full Length of Mature Protein of Isoform 2
Activity: Not Tested

Expression system: HEK293 Cells
Length: 19-261, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-85, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 25-413, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 20-397, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 21-418, Full Length of Mature Protein
Activity: Not Tested