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63013

Sigma-Aldrich

α2-Macroglobulin from human plasma

≥90% (GE)

Synonym(s):

α2-M

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About This Item

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

biological source

human plasma

Quality Level

Assay

≥90% (GE)

mol wt

~720 kDa (four glycoprotein subunits)

technique(s)

cell culture | mammalian: suitable

solubility

H2O: 1 mg/mL, clear to faintly turbid, colorless to faintly yellow

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... A2M(2)

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Application

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 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.

Analysis Note

100 mg solids are lyophilized with 1 mg glycine from 35.2 mL 30 mM sodium phosphate, pH 7.0
Plasma from each donor has been tested and found negative for antibody to HIV-1/HIV-2, antibody to HCV and HbSAg.

Other Notes

Conformational changes of α2-M

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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P A Roche et al.
Biochemistry, 28(19), 7629-7636 (1989-09-19)
Treatment of the human plasma proteinase inhibitor alpha 2-macroglobulin (alpha 2M) with proteinase results in conformational changes in the inhibitor and subsequent activation and cleavage of the internal thiolester bonds of alpha 2M. Previous studies from this laboratory have shown
Alpha 2-macroglobulin.
H Ishibashi et al.
Methods in enzymology, 163, 485-495 (1988-01-01)
Paul Dent et al.
Journal of cellular physiology, 235(10), 6862-6874 (2020-01-28)
We have extended our analyses of (curcumin+sildenafil) biology. The drug combination caused vascularization and degradation of mutant K-RAS that correlated with reduced phosphorylation of ERK1/2, AKT T308, mTORC1, mTORC2, ULK1 S757, STAT3, STAT5, and NFκB and increased phosphorylation of eIF2α
Yonathan Uriel et al.
Insect science, 27(2), 256-265 (2018-07-27)
We tested the recent hypothesis that the "fly factor" phenomenon (food currently or previously fed on by flies attracts more flies than the same type of food kept inaccessible to flies) is mediated by bacterial symbionts deposited with feces or
J J Feige et al.
Hormone research, 45(3-5), 227-232 (1996-01-01)
alpha 2-Macroglobulin (alpha 2M) is a large plasma glycoprotein that has long been known as an irreversible inhibitor of a variety of proteinases. More recently, it has been reported that numerous growth factors, cytokines and hormones bind to alpha 2M

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