Apolipoprotein H, Human (beta 2 Glycoprotein 1, ApoHb2gp1)

Apolipoprotein H (b2-Glycoprotein I, b2I) is a highly glycosylated single chain protein (Mr=54,200) which is synthesized in the liver and circulates in plasma at a concentration of 100-200ug/ml (1-4). Approximately 40% of the plasma b2I is associated with lipoproteins, which led to the designation apolipoprotein H (5). The 326 amino acid protein contains five repeating mutually homologous domains consisting of approximately 60 amino acids which are disulfide bonded to form Short Consensus Repeats (SCR) or Sushi domains. The third, C-terminal sushi domain contains three of the five N-linked carbohydrate chains, at positions N143, N164, N174. The other two sites are at N73 and N234 in domains II and IV, respectively. There are 38 basic amino acid residues distributed unevenly among the five domains; eight in domain I, five in domain II, five in domain III, five in domain IV and fifteen in domain V. The direct binding of domains I and V has been demonstrated and likely results from folding of the molecule in a manner that expresses a net cationic surface charge (5). \n\nAlthough the physiological role of Apolipoprotein H is still being studied, the ability to bind to anionic surfaces has been the focus of intense investigation. Apolipoprotein H has been shown to bind to anionic vesicles (3), platelets (6), DNA (7), mitochondria (8) and heparin (9). It has been suggested that the binding of Apolipoprotein H to negatively charged surfaces can inhibit the contact activation pathway in blood coagulation. The binding to activated platelets is reported to inhibit platelet associated prothrombinase and adenylate cyclase activities. Studies on physiologic roles for binding to DNA, mitochondria, heparanoids and phospholipids have focused on the area of autoimmune disorders. In particular, the complexes between Apolipoprotein H and cardiolipin have been implicated in the anti-phospholipid related disorders LAC and SLE (10-13).\n\nStorage and Stability: May be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.\n\nAdditional Specifications:\nLocalization: Plasma\n\nPlasma Concentration: 100-200ug/ml\n\nMode of Action: Cationic residues on the surface of sushi domains I and V bind to anionic phospholipids. Inhibition of contact activation, platelet membrane dependent prothrombinase and adenylate cyclase activities. Complexes with DNA, mitochondria, and cardiolipin augments antigenicity in autoimmune disorders.\n\nMolecular Weight: 54,200 (SDS PAGE), 48,000 (Sed. Equil)\n\nExtinction Coefficient: E1%1cm, 280nm=10.0\n\nStructure: 326 amino acid single chain protein with 5 contiguous Short Consensus Repeats on sushi domains.\n\nPercent Carbohydrate: 25%\n\nPost-translational Modifications: 5 N-linked glycosylation sites, 1 in domain II (N73), 3 in domain III (N143, N164, N174) and 1 in domain IV (N224).

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SPECIFICATIONS

Catalog Number

A2299-77E

Size

100ug

Form

Supplied lyophilized from glycine buffered saline.

Purity

The human Apolipoprotein H is purified from fresh frozen human plasma, using a combination of ion exchange and affinity chromatography. It is greater than 95% pure by SDS PAGE.

References

US Biological application references: 1. Zhou, H. et al.., (2012) Thrombosis Research http://dx.doi.org/10.1016/j.thromres.2012.08.303. 2. Xie, H. et al., (2012) Molecular Immunology 53; 246-254. 3. Zhou, H. et al., (2013) Thrombosis Research, http://dx.doi.org/10.1016/j.thromres.2013.09.039. 1. Lozier, J., et.al., Proc.Natl.Acad. Sci.,USA, 81, 2640-3644 (1984). 2. Kato, H. and Enjyoi, K., Biochem., 30, 11687-11694 (1997). 3. Wurm, H., Int.J.Biochem., 16, 511-515 (1984). 4. Bendixen, E., et.al., Biochem., 31, 3611-3617 (1992). 5. Steinkasserer, A., et.al., Biochem.J., 277, 387-391 (1991). 6. Nimpf, J. et.al., Biochim.Biophys.Acta, 884, 142-149 (1986). 7. Kroll, J. et.al., Biochim.Biophys.Acta, 434, 490-501 (1986). 8. Schousboe, I., Biochim.Biophys.Acta, 679, 396-408 (1979). 9. Polz, E., et.al., Int.J.Biochim., 11, 265-273 (1076). 10. McNeil, H.P. et.al., Proc.Natl.Acad.USA, 87, 4120-4124 (1990). 11. Galli, M. et.al., Lancet, I, 1544-1547 (1990). 12. Matsuuna, E., et.al., Lancet, II, 177-178 (1990). 13. Pengo, V. et.al., Thrombosis and Haemostasis, 73, 29-34 (1995).