M6159
α2-Macroglobulin from human plasma
BioUltra, ≥98% (SDS-PAGE)
Synonym(s):
α2-M
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About This Item
Product Name
α2-Macroglobulin from human plasma, BioUltra, ≥98% (SDS-PAGE)
biological source
human plasma
product line
BioUltra
assay
≥98% (SDS-PAGE)
form
lyophilized powder
mol wt
~720 kDa (four glycoprotein subunits)
composition
Protein, 15-30% biuret
technique(s)
inhibition assay: suitable
solubility
water: soluble 10 mg protein/mL, clear, colorless
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
human ... A2M(2)
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Analysis Note
Plasma from each donor has been tested and found negative for antibody to HIV-1/HIV-2, antibody to HCV and HbSAg.
Application
α2-Macroglobulin was used to study impaired lipoprotein receptor-mediated peripheral binding of plasma amyloid-β which is an early biomarker for mild cognitive impairment preceding Alzheimer′s disease. It was also used in the control of the classical and the MBL pathway of complement activation.
Inhibits all classes of endoproteases by forming a complex with the protease. When the protease cleaves the macroglobulin "bait" sequence, the macroglobulin rearranges and traps the protease.
Biochem/physiol Actions
α2-Macroglobulin (α2M) is a multifunctional protein that is a broad spectrum protease inhibitor. α2M is a large homotetrameric glycoprotein (720 kDa) that is connected by disulfide-linked dimers which non-covalently interact to give the quaternary structure. α2M is found in normal plasma at a concentration of 220-230 mg/dl accounting for 3-5% of the total plasma protein.
α2-Macroglobulin is found abundantly in plasma and interstitial fluids. The protease-α2-M balance plays an important role in mediating inflammatory tissue destruction. Serum levels of α2-M and protease-α2-M complexes are increased in patients with sepsis, emphysema, periodontitis, rheumatoid arthritis, and other inflammatory diseases, and oxidant inactivation of α2-M may contribute to tissue destruction during inflammation.
Serum levels of α2-Macroglobulin (α2-M) and protease-α2-M complexes are increased in patients with sepsis, emphysema, periodontitis, rheumatoid arthritis and other inflammatory diseases. It is hypothesized that the oxidant inactivation of α2-M contributes to tissue destruction in inflammation.
Packaging
Package size based on protein content
Physical form
Lyophilized from 0.02 M Tris, 0.13 M glycine, pH 8.0, and 0.08 M trehalose
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Changqi Sun et al.
Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 41(1), 241-248 (2022-04-23)
A hallmark of osteoarthritis (OA) is cartilage degeneration, which has been previously correlated with dramatic increases in inflammatory enzymes. Specifically, interleukin-1β (IL-1β) and subsequent upregulation of nuclear factor kappa B (NF-κB) is implicated as an important player in the development
E M Smergel et al.
Clinical nuclear medicine, 12(5), 349-353 (1987-05-01)
Fourteen patients with slipped capital femoral epiphysis (SCFE) who had high-resolution and magnification bone scintigraphy during treatment were studied. By demonstrating the vascular status of the femoral head and physiologic condition of the growth plate, scintigraphy was found to assist
Osama A Hamad et al.
Journal of immunology (Baltimore, Md. : 1950), 184(5), 2686-2692 (2010-02-09)
It has been reported that complement is activated on the surface of activated platelets, despite the presence of multiple regulators of complement activation. To reinvestigate the mechanisms by which activated platelets bind to complement components, the presence of complement proteins
Structural characterization of human alpha2-macroglobulin subunits.
R P Swenson et al.
The Journal of biological chemistry, 254(11), 4452-4456 (1979-06-10)
Wen-Feng Zeng et al.
Scientific reports, 6, 25102-25102 (2016-05-04)
Confident characterization of the microheterogeneity of protein glycosylation through identification of intact glycopeptides remains one of the toughest analytical challenges for glycoproteomics. Recently proposed mass spectrometry (MS)-based methods still have some defects such as lack of the false discovery rate
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