Recombinant Human alpha 2 Macroglobulin protein
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Recombinant Human alpha 2 Macroglobulin protein is a Human Fragment protein, in the 641 to 730 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
CPAMD5, FWP007, A2M, Alpha-2-macroglobulin, Alpha-2-M, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human alpha 2 Macroglobulin protein (AB157817)
ab157817 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Alpha-2-macroglobulin plays an important role in maintaining homeostasis by regulating protease activities and modulating immune system reactions. It does not form a permanent complex but can transiently associate with the proteases and various molecules mentioned. By interacting with proteases it controls processes like coagulation and fibrinolysis and participates in the clearance of proteinases and growth factors from the circulation. It influences cell signaling pathways and inflammatory responses highlighting its significance in maintaining balance within the body.
Pathways
Alpha-2-macroglobulin is an important component in the immune response and coagulation pathways. In the complement system it binds with complement components to regulate their activities. It associates with proteins such as plasmin and thrombin which are important for blood clotting and fibrinolysis. These relationships emphasize the protein's involvement in both protective mechanisms against pathogens and the regulation of blood coagulation and breakdown connecting the immune and hemostatic systems.
Specifications
Form
Liquid
General info
Function
Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
Sequence similarities
Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family.
Target data
Product promise
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