This alpha 2 Macroglobulin antibody is un-conjugated
Application
Immunohistochemistry (IHC)
Purification
Purified by antigen-specific affinity chromatography.
Immunogen
Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human A2M (Alpha-2-macroglobulin precursor)
A2M
Reactivity: Human
WB, ELISA
Host: Goat
Polyclonal
Biotin
Application Notes
ELISA, Western blotting: 1µg/ml for 2hrs.
Restrictions
For Research Use only
Format
Liquid
Buffer
This antibody is stored in PBS, 50% glycerol
Preservative
Sodium azide
Precaution of Use
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Zhang, Li, Martin, Aebersold: "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." in: Nature biotechnology, Vol. 21, Issue 6, pp. 660-6, (2003) (PubMed).
Matthijs, Devriendt, Cassiman, Van den Berghe, Marynen: "Structure of the human alpha-2 macroglobulin gene and its promotor." in: Biochemical and biophysical research communications, Vol. 184, Issue 2, pp. 596-603, (1992) (PubMed).
Bishop, Bell: "Assembly of the endoplasmic reticulum phospholipid bilayer: the phosphatidylcholine transporter." in: Cell, Vol. 42, Issue 1, pp. 51-60, (1985) (PubMed).
Sottrup-Jensen, Stepanik, Kristensen, Wierzbicki, Jones, Lønblad, Magnusson, Petersen: "Primary structure of human alpha 2-macroglobulin. V. The complete structure." in: The Journal of biological chemistry, Vol. 259, Issue 13, pp. 8318-27, (1984) (PubMed).
Sottrup-Jensen, Lønblad, Stepanik, Petersen, Magnusson, Jörnvall: "Primary structure of the 'bait' region for proteinases in alpha 2-macroglobulin. Nature of the complex." in: FEBS letters, Vol. 127, Issue 2, pp. 167-73, (1981) (PubMed).
A2M (Alpha-2-macroglobulin) is able to inhibit all four classes of proteinases by a unique `trapping' mechanism. This protein has a peptide stretch, called the `bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.