Abcam, ab229370, Recombinant human Serpin A5 protein (Active)

Size: 10µg
Recombinant human Serpin A5 protein (Active) is a Human Full Length protein, in the 20 to 406 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS, Mass Spec.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, FuncS, Mass SpecSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.,
Accession:P05154,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 6Constituents: 10% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.39% MES

Product details:
Previously labelled as Protein C inhibitor.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
Biological function summary
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.
Pathways
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.