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Merck

M6159

α2-Macroglobulin from human plasma

BioUltra, ≥98% (SDS-PAGE)

Sinónimos:

α2-M

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Número CAS:
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
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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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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.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
Structural characterization of human alpha2-macroglobulin subunits.
R P Swenson et al.
The Journal of biological chemistry, 254(11), 4452-4456 (1979-06-10)
Osama A Hamad et al.
Journal of immunology (Baltimore, Md. : 1950), 184(5), 2686-2692 (2010-02-09)
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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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