Recombinant Mouse Apolipoprotein H Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Apolipoprotein H Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA.

When Recombinant Mouse Apolipoprotein H/ApoH is immobilized at 2 μg/mL, 100 μL/well, the concentration of Recombinant Mouse LDL R (Catalog # 2255-LD) that produces 50% of the optimal binding response is found to be approximately 0.05-0.25 μg/mL.

Source
Mouse myeloma cell line, NS0-derived mouse Apolipoprotein H/ApoH protein
Gly20-Cys345, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gly20
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
Apoh
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
37.5 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60-65 kDa, reducing conditions
Publications
Read Publications using
6575-AH in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Apolipoprotein H Protein, CF

  • Activated protein C-binding protein
  • Anticardiolipin cofactor
  • APC inhibitor
  • APOH
  • apo-H
  • apolipoprotein H (beta-2-glycoprotein I)
  • Apolipoprotein H
  • B2G1
  • B2GP1
  • B2GPI
  • Beta
  • beta(2)GPI
  • beta-2-glycoprotein 1
  • Beta-2-glycoprotein I
  • BG

Background

Apolipoprotein H (ApoH), also known as beta 2‑Glycoprotein I/ beta 2-GPI, is a 50 kDa variably glycosylated member of the complement control superfamily of proteins (1, 2). Mature mouse ApoH consists of four tandem Sushi/SCR repeats followed by one Sushi-like repeat (3, 4). Mature mouse ApoH shares 76% and 42% aa sequence identity with human and rat ApoH, respectively. Hepatocyte-derived ApoH binds directly to negatively charged phospholipids (5). It circulates as a component of lipoprotein particles and as a lipid-free serum protein (6). ApoH also associates with liposomes and apoptotic cell debris, thereby enabling their renal clearance via Megalin uptake (7, 8). Circulating levels of ApoH are postively correlated with triglyceride-rich lipoprotein (VLDL) components in type II diabetes (9). ApoH inhibits thrombosis by blocking the activation of Coagulation Factor XI but also shows procoagulant activity by inhibiting the activation of Protein C (10, 11). ApoH can be cleaved by Plasmin at Lys317 ‑ Thr318, an action that is enhanced by heparin (12, 13). ApoH cleavage reduces its ability to bind phospholipids and inhibit Factor XI activation but confers the ability to bind Plasminogen (10, 12, 14). Cleaved ApoH also demonstrates antiangiogenic activity, whereas intact ApoH does not (14). The production of antibodies against ApoH is a hallmark of Antiphospholipid Syndrome (APS), an autoimmune disorder that leads to hypercoagulability and recurrent miscarriages (15). ApoH binds to the surface antigen of Hepatitis B Virus and is associated with the development of HBV-induced hepatocellular carcinoma (6, 16).
  1. Crook, M.A. et al. (2010) Atherosclerosis 209:32.
  2. Miyakis, S. et al. (2004) Thromb. Res. 114:335.
  3. Nonaka, M. et al. (1992) Genomics 13:1082.
  4. Lozier, J. et al. (1984) Proc. Natl. Acad. Sci. 81:3640.
  5. Wurm, H. (1984) Int. J. Biochem. 16:511.
  6. Mehdi, H. et al. (1994) J. Virol. 68:2415.
  7. Chonn, A. et al. (1995) J. Biol. Chem. 270:25845.
  8. Moestrup, S.K. et al. (1998) J. Clin. Invest. 102:902.
  9. Castro, A. et al. (2010) Atherosclerosis 209:201.
  10. Shi, T. et al. (2004) Proc. Natl. Acad. Sci. 101:3939.
  11. Mori, T. et al. (1996) Thromb. Haemost. 75:49.
  12. Hunt, J. et al. (1993) Proc. Natl. Acad. Sci. 90:2141.
  13. Guerin, J. et al. (2002) J. Biol. Chem. 277:2644.
  14. Sakai, T. et al. (2007) Am. J. Pathol. 171:1659.
  15. Adams, M. (2008) Semin. Thromb. Haemost. 34:251.
  16. Jing, X. et al. (2010) J. Cancer Res. Clin. Oncol. 16:1671.

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Publications for Apolipoprotein H/ApoH (6575-AH)(3)

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Bioinformatics

Gene Symbol Apoh
Uniprot