Recombinant Human Serpin A5 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.
PCI, PLANH3, PROCI, SERPINA5, Plasma serine protease inhibitor, Acrosomal serine protease inhibitor, Plasminogen activator inhibitor 3, Protein C inhibitor, Serpin A5, PAI-3, PAI3
Recombinant Human Serpin A5 protein is a Human Full Length protein, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 6
Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab89362 is purified using conventional chromatography techniques.
Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid.
Belongs to the serpin family.
N- and O-glycosylated. N-glycosylation consists of a mixture of sialylated bi- (including sialyl-Lewis X epitopes), tri- and tetra-antennary complex-type chains; affects the maximal heparin- and thrombomodulin-enhanced rates of thrombin inhibition. O-glycosylated with core 1 or possibly core 8 glycans. Further modified with 2 sialic acid residues.
Previously labelled as Protein C inhibitor.
Serpin A5 also known as Protein C Inhibitor (PCI) or Mesotrypsin inhibitor is a member of the serine protease inhibitor family with a mass of approximately 47 kDa. It plays a mechanical role as an inhibitor of several proteases such as trypsin tissue-type plasminogen activator and urokinase-type plasminogen activator. This protein is highly expressed in tissues including the liver kidneys and seminal plasma suggesting its involvement in reproductive and hemostatic processes.
Serpin A5 regulates critical physiological processes through its inhibitory function. It interacts with and inhibits target proteases controlling pathways involved in coagulation and fibrinolysis. Serpin A5 does not form part of larger protein complexes but exerts its function through direct interactions. Its modulatory action impacts processes such as cell migration and tumor invasion highlighting its role in broader cellular environments.
Serpin A5 is an important regulator in the coagulation cascade and fibrinolytic pathways. It acts to modulate the balance between coagulation and fibrinolysis critical for maintaining hemostasis. This protein is related to other serpins such as Antithrombin III and Plasminogen activator inhibitor-1 through its regulatory actions in these pathways. The inhibition of proteases by Serpin A5 ensures proper activation and termination of these biological processes which are essential for vascular integrity.
Serpin A5 is connected to conditions like thrombophilia and prostate cancer. Dysregulation in its expression or function leads to altered coagulation increasing the risk of thrombotic events. In prostate cancer its role is linked through pathways involving the matrix metalloproteinases where Serpin A5 can influence tumor progression and metastasis. Understanding its interactions with proteins in these diseases provides insights into potential therapeutic strategies.
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3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
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