antibody

Goat anti-human alpha2Macroglobulin (alpha2M), Whole IgG from antiserum

MBS512010

10 mg

230 USD

polyclonal

goat

nonconjugated

Antibody

Goat anti-human alpha2Macroglobulin (alpha2M), Whole IgG from antiserum

alpha2-Macroglobulin

alpha2-Macroglobulin, human

Alpha-2-macroglobulin; Alpha-2-macroglobulin; alpha-2-macroglobulin; alpha-2-M; OTTHUMP00000196829; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5; alpha-2-macroglobulin; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5

A2M; A2M; A2MD; CPAMD5; FWP007; S863-7; DKFZp779B086; CPAMD5

A2MG_HUMAN

Polyclonal

Goat

This antibody is specific for alpha2macroglobulin as demonstrated by immunoelectrophoresis and ELISA.

Purified IgG. Vial containing ml of whole IgG, representing approximately 1 ml of antiserum. Total protein is 10 mg.

Whole IgG, clear liquid.

IgG concentration is mg/ml, determined by absorbance using an extinction coefficient (E1%280) of 13.4.

Store between -10 and -20 degree C. Product will become viscous but will not freeze. Avoid storage in frost-free freezers. Keep vial tightly capped. Allow product to warm to room temperature and gently mix before use.

Suitable for use as a source of antibodies to human alpha2M.

Immunogen: Human alpha2macroglobulin purified from plasma.

Buffer: 10 mM HEPES, pH 7.4, 150 mM NaCl, 50% (v/v) glycerol. Neutralizing Activity: Not determined

alpha2Macroglobulin (alpha2M) is a large proteinase inhibitor molecule of 718,000 daltons, consisting of 4 identical subunits of 185,000 each. Produced in hepatocytes and macrophages, plasma concentrations of alpha2M are typically 2 uM in adults, and as high as 6 uM in childhood. alpha2M has the ability to inhibit most enzymes from the serine, metallo, cysteine and aspartate subclasses. It is not a member of the SERPIN family of inhibitors but belongs to a class of proteins that include pregnancy zone protein (PZP) and the complement proteins C3, C4 and C5. These proteins contain regions of conserved sequence as well as one or more internal beta-cysteinyl-gamma- glutamyl thiolester bonds, which in the case of alpha2M are susceptible to cleavage by enzymes or by nucleophilic compounds such as methylamine or ammonium ions. Although the precise nature of the interactions is as yet unknown, it is generally thought that cleavage of a bait region within the alpha2M molecule by an enzyme leads to a conformational change, which then traps and/or covalently binds the enzyme1,2. The active site of the trapped enzyme is usually still intact and able to cleave small substrates, but is inaccessible to larger natural substrates. The conformational change induced also exposes receptor-binding regions within the molecule, which may be important in the clearance of alpha2M-enzyme complexes from the circulation. It is thought that the main role of alpha2M in vivo is that of a "backup" inhibitor and scavenger of proteinases in blood and in tissues3,4, but it has also been reported to participate in other physiological processes, including regulation of immune function1,2.

1. Salvesen G, Pizzo SV; Proteinase Inhibitors: alpha-Macroglobulins, Serpins and Kunins; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp. 241-258, J.B. Lippincott Co., Philadelphia PA, USA, 1994. 2. Barrett J; alpha2Macroglobulin; Methods in Enzymology, 80, pp 737-754, 1981 Larsson LJ, Neuenschwander DE, Strickland DK; Reaction of Proteinases with alpha2Macroglobulin: Evidence for Alternate Reaction Pathways in the Inhibition of Trypsin; Biochemistry 28, pp 7636-7643, 1989. 3. Schmidt B, Mitchell L, Ofosu FA, Andrew M; alpha2Macroglobulin is an Important Progressive Inhibitor of Thrombin in Neonatal and Infant Plasma; Thromb Haemostas 62, pp 1074-1077, 1989. 4. Hoogendoorn H, Toh CH, Nesheim ME, Giles AR; alpha2Macroglobulin Binds and Inhibits Activated Protein C; Blood 78, pp2283-2290, 1991.

112911

P01023.1

P01023

P01023

163,291 Da

Complement And Coagulation Cascades Pathway (198880); Complement And Coagulation Cascades Pathway (83073); Complement And Coagulation Cascades Pathway (484); Formation Of Fibrin Clot (Clotting Cascade) Pathway (106057); Formation Of Platelet Plug Pathway (106029); HDL-mediated Lipid Transport Pathway (106158); Hemostasis Pathway (106028); IL6-mediated Signaling Events Pathway (137932); Intrinsic Pathway (106059); Lipid Digestion, Mobilization, And Transport Pathway (106111)

Alpha-2-macroglobulin is a protease inhibitor and cytokine transporter. It inhibits many proteases, including trypsin, thrombin and collagenase. A2M is implicated in Alzheimer disease (AD) due to its ability to mediate the clearance and degradation of A-beta, the major component of beta-amyloid deposits. [provided by RefSeq]

Function: 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 thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase. Subunit structure: Homotetramer; disulfide-linked. Ref.8 Ref.10. Subcellular location: Secreted Ref.8. Tissue specificity: Secreted in plasma. Ref.8. Developmental stage: Contrary to the rat protein, which is an acute phase protein, this protein is always present at high levels in circulation. Sequence similarities: Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family. [View classification]. Sequence caution: The sequence AAT02228.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence BAD92851.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

10 mg

230 USD