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M6159

Sigma-Aldrich

α2-Macroglobulin from human plasma

BioUltra, ≥98% (SDS-PAGE)

Synonym(s):

α2-M

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About This Item

CAS Number:
1631137-21-7
MDL number:
MFCD00130472
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

human plasma

Quality Level

200

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.

P01023

storage temp.

−20°C

Gene Information

human ... A2M(2)

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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

Analysis Note

Plasma from each donor has been tested and found negative for antibody to HIV-1/HIV-2, antibody to HCV and HbSAg.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
SLCK1756
SLCJ1769
SLCH2624
SLCG8164
SLCF9449

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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
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
Structural characterization of human alpha2-macroglobulin subunits.
R P Swenson et al.
The Journal of biological chemistry, 254(11), 4452-4456 (1979-06-10)
S V Petersen et al.
Molecular immunology, 37(14), 803-811 (2001-03-21)
The activation of complement via the mannan-binding lectin (MBL) pathway is initiated by the MBL complex consisting of the carbohydrate binding molecule, MBL, two associated serine proteases, MASP-1 and MASP-2, and a third protein, MAp19. In the present report we
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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