protein

NATIVE HUMAN ALPHA 2 MACROGLOBULIN

MBS230187

1 mg

365 USD

Purified Protein

NATIVE HUMAN ALPHA 2 MACROGLOBULIN

ALPHA 2 MACROGLOBULIN

alpha-2-macroglobulin; Alpha-2-macroglobulin; alpha-2-macroglobulin; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5; alpha-2-M; alpha-2-macroglobulin; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5

A2M; A2M; A2MD; CPAMD5; FWP007; S863-7; CPAMD5; Alpha-2-M

A2MG_HUMAN

1,474

>96% by SDS PAGE

Purified. Purified alpha-2-macroglobulin from human serum - liquid

Total protein concentration 1.0 mg/ml

Store at -20 degree C only. Storage in frost-free freezers is not recommended. This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the protein. Shelf Life: 12 months from date of despatch.

ELISA (EIA)

Perservative Stabilisers: 0.1M Sucrose

Buffer Solution: TRIS buffered saline. Target Species: Human

Alpha-2-Macroglobulin, also known as a2-macroglobulin and abbreviated as a2M and A2M, is a tetrameric glycoprotein produced in the liver and found in blood. It is involved in proteinase inhibition via a unique "trapping" mechanism.

66932947

NP_000005.2

NM_000014.4

P01023

725 kDa

Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); Degradation Of The Extracellular Matrix Pathway (576263); Extracellular Matrix Organization Pathway (576262); Formation Of Fibrin Clot (Clotting Cascade) Pathway (106057); HDL-mediated Lipid Transport Pathway (106158); Hemostasis Pathway (106028); IL6-mediated Signaling Events Pathway (137932); Intrinsic Pathway (106059)

Alpha-2-macroglobulin is a protease inhibitor and cytokine transporter. It inhibits many proteases, including trypsin, thrombin and collagenase. A2M is implicated in Alzheimer disease (AD) due to its ability to mediate the clearance and degradation of A-beta, the major component of beta-amyloid deposits. [provided by RefSeq, Jul 2008]

A2M: 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. Belongs to the protease inhibitor I39 (alpha-2- macroglobulin) family. Protein type: Secreted; Inhibitor; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 12p13.31. Cellular Component: extracellular region; cytosol. Molecular Function: serine-type endopeptidase inhibitor activity; protein binding; enzyme binding; protease binding; growth factor binding; interleukin-8 binding; interleukin-1 binding; calcium-dependent protein binding; tumor necrosis factor binding; receptor binding. Biological Process: negative regulation of complement activation, lectin pathway; platelet activation; extracellular matrix disassembly; extracellular matrix organization and biogenesis; regulation of small GTPase mediated signal transduction; platelet degranulation; small GTPase mediated signal transduction; stem cell differentiation; blood coagulation; blood coagulation, intrinsic pathway. Disease: Alzheimer Disease; Alpha-2-macroglobulin Deficiency

1 mg

365 USD