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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
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
常规特殊物品
Certificates of Analysis (COA)
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Paul Dent et al.
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Alpha 2-macroglobulin.
H Ishibashi et al.
Methods in enzymology, 163, 485-495 (1988-01-01)
Yonathan Uriel et al.
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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
M Luo et al.
Journal of thrombosis and haemostasis : JTH, 15(12), 2451-2460 (2017-10-14)
Essentials Vitronectin (VN) is produced by smooth muscle cells (SMCs) and promotes neointima formation. We studied the regulation of vascular VN expression by plasminogen activator inhibitor-1 (PAI-1). PAI-1 stimulates VN gene expression in SMCs by binding LDL receptor-related protein 1.
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