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alpha 2 Macroglobulin antibody (alpha-2-Macroglobulin) (C-Term)

Details for Product anti-A2M Antibody No. ABIN965491, Supplier: Log in to see
Antigen
  • A2M
  • LOC733429
  • LOC100221148
  • LOC100224071
  • endod
  • cpamd5
  • fwp007
  • s863-7
  • a2mb
  • endodermin
  • A2MD
  • CPAMD5
  • FWP007
  • S863-7
  • A2mp
  • A2MAC1
  • A2m1
  • A2maa
  • Mam
  • alpha-2-macroglobulin
  • ovostatin
  • pregnancy-zone protein
  • A2M
  • LOC733429
  • AZL_c00450
  • LOC100221148
  • LOC100224071
  • LOC100349077
  • OVST
  • a2m
  • A2m
  • LOC100353095
  • PZP
Epitope
C-Term
23
15
15
14
11
7
5
5
5
5
5
5
5
5
4
3
3
3
3
1
1
1
1
Reactivity
Human
196
37
37
8
7
5
3
3
2
1
Host
Rabbit
131
74
37
8
5
4
2
Clonality
Polyclonal
Conjugate
This alpha 2 Macroglobulin antibody is un-conjugated
23
15
13
6
6
6
Application
Immunohistochemistry (IHC)
182
181
53
45
24
13
12
10
10
7
6
5
3
1
1
1
1
Options
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human A2M (Alpha-2-macroglobulin precursor)
Purification Purified by antigen-specific affinity chromatography.
Alternative Name A2M (A2M Antibody Abstract)
Background 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.
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
Background publications 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).

Huang, Dolmer, Liao, Gettins: "Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin." in: Protein science : a publication of the Protein Society, Vol. 7, Issue 12, pp. 2602-12, 1999 (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).

Poller, Faber, Klobeck, Olek: "Cloning of the human alpha 2-macroglobulin gene and detection of mutations in two functional domains: the bait region and the thiolester site." in: Human genetics, Vol. 88, Issue 3, pp. 313-9, 1992 (PubMed).

Bell, Rall, Sanchez-Pescador, Merryweather, Scott, Eddy, Shows: "Human alpha 2-macroglobulin gene is located on chromosome 12." in: Somatic cell and molecular genetics, Vol. 11, Issue 3, pp. 285-9, 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).

Hall, Nelles, Travis, Roberts: "Proteolytic cleavage sites on alpha 2-macroglobulin resulting in proteinase binding are different for trypsin and Staphylococcus aureus V-8 proteinase." in: Biochemical and biophysical research communications, Vol. 100, Issue 1, pp. 8-16, 1981 (PubMed).

Product cited in: Bishop, Bell: "Assembly of the endoplasmic reticulum phospholipid bilayer: the phosphatidylcholine transporter." in: Cell, Vol. 42, Issue 1, pp. 51-60, 1985 (PubMed).