M6159
 |   |  |
 | α2-Macroglobulin is a tetramer with four identical subunits with molecular weights of 179 kDa. Upon binding to a protease, the 179 kDa subunit is cleaved into two 85 kDa fragments. |
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M6159
Sigma
α2-Macroglobulin from human plasma
BioUltra, lyophilized powder, ≥98% (SDS-PAGE)
| Synonym: | α2-M |
| MDL number: | MFCD00130472 |
Description
| Analysis Note | Plasma from each donor has been tested and found negative for antibody to HIV-1/HIV-2, antibody to HCV and HbSAg. |
| One mg of α2-macroglobulin will inhibit a minimum of 10 μg trypsin with an activity of 10,000 BAEE un/mg protein | |
| Application | Inhibits all classes of endoproteases by forming a 1:1 complex with the protease. When the protease cleaves the macroglobulin “bait” sequence, the macroglobulin rearranges and traps the protease. |
| 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 |
| Biochem/physiol Actions | α2-Macroglobulin is found abundantly in plasma and interstitial fluids. The protease-α2-M balance plays an important role in mediating inflammation-associated 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. It is hypothesized that the oxidant inactivation of α2-M contributes to tissue destruction during inflammation. α2-M has been implicated as a genetic risk factor for late-onset Alzheimer's disease. Activated α2-M enhances the clearance of soluble α/β-amyloid via low-density lipoprotein receptor-related protein in cortical neurons, but has no effect on secreted or full-length APP levels. |
Properties
| grade | BioUltra |
| assay | ≥98% (SDS-PAGE) |
| form | lyophilized powder |
| mol wt | mol wt ~720 kDa (four glycoprotein subunits) |
| composition | Protein, 15-30% biuret |
| Gene Information | human ... A2M(2) |
| storage temp. | −20°C |
Safety
| Hazard Codes | B |
| WGK Germany | 3 |
References
| reference | Barrett, A.M. Meth. Enzymol. 80, 737, (1981) |
| Kurecki, T., et al. Anal. Biochem. 99, 415, (1979) | |
| Salvesen, G. and Enghild, J.J. Meth. Enzymol. 223, 121, (1993) | |
| Wu, S.M. and Pizzo, S.V. Biochemistry 38, 13983, (1999) | |
| Qiu, Z., et al. J. Neurochem. 73, 1393, (1999) |
