protein

Alpha-1 Macroglobulin, Mouse Serum

MBS173012

0.1 mg

395 USD

Protein

Alpha-1 Macroglobulin, Mouse Serum

[Alpha-2-Macroglobulin]

[Alpha-1 Macroglobulin (A1M), Mouse, A2M, AMG]

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

Mouse serum

1474

> 95% (SDS-PAGE, major bands at 160 and 35 kDa).

Solution in 0.01 M sodium phosphate, 0.15M sodium chloride, 0.1% sodium azide, pH 7.2

Store at -70°C. Avoid freeze/ thaws. Ships in Dry Ice.

Appearance: Frozen solution . Protein: 3.6 mg/mL (Coomassie).

Handling: Handle as a potentially hazardous substance. Recovery: Centrifuge briefly to ensure complete recovery.

Proteins; Antigens; Standards/controls; Native Proteins; Alpha-2 Macroglobulin (a2m)

66932947

NP_000005.2

NM_000014.4

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, signal peptide; Secreted; Inhibitor. 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; regulation of small GTPase mediated signal transduction; extracellular matrix organization and biogenesis; platelet degranulation; small GTPase mediated signal transduction; stem cell differentiation; blood coagulation; blood coagulation, intrinsic pathway. Disease: Alzheimer Disease; Alpha-2-macroglobulin Deficiency

0.1 mg

395 USD

1 mg

1645