Recombinant Human Apolipoprotein M Protein, CF

R&D Systems | Catalog # 4550-AM

R&D Systems
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Key Product Details

  • R&D Systems E. coli-derived Recombinant Human Apolipoprotein M Protein (4550-AM)
  • Quality control testing to verify active proteins with lot specific assays by in-house scientists
  • All R&D Systems proteins are covered with a 100% guarantee

Source

E. coli

Accession Number

Applications

Bioactivity
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Product Specifications

Source

E. coli-derived human Apolipoprotein M/ApoM protein
Cys23-Asn188, with an N-terminal Met and 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met & Thr62

Predicted Molecular Mass

19.5 kDa

SDS-PAGE

19-21 kDa, reducing conditions

Activity

Measured by its ability to bind all-trans-retinoic acid. The concentration of all-trans-retinoic acid required to quench 50% of Trp fluorescence in Recombinant Human Apolipoprotein M/ApoM is approximately 10-50 μM.

Reviewed Applications

Read 1 review rated 5 using 4550-AM in the following applications:

Formulation, Preparation, and Storage

4550-AM
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution

Reconstitute at 500 μg/mL in PBS.


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Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Apolipoprotein M/ApoM

Apolipoprotein M (ApoM) is an approximately 25 kDa variably glycosylated protein that adopts a beta-barrel structure characteristic of lipocalin family proteins. It functions as a component of lipoprotein particles which play essential roles in fatty acid and cholesterol transport and metabolism (1, 2). Human ApoM shares 83% amino acid sequence identity with mouse and rat ApoM (3). Alternative splicing generates a short isoform that lacks the N-terminal 72 amino acids. ApoM is produced primarily by hepatocytes but also by renal tubule epithelial cells (4). The signal peptide is not cleaved and is required for ApoM association with lipoprotein particles as well as Megalin mediated reabsorption by the kidney (5, 6). ApoM is cleared from the circulation by the ubiquitously expressed LDL R (7, 8). The majority of circulating ApoM is associated with HDL, while a smaller fraction is associated with LDL (3, 9, 10). It promotes the intracellular formation of large pre-beta (discoidal) HDL particles which inhibit the development of atherosclerotic plaques by facilitating the efflux of cellular cholesterol and preventing phospholipid oxidation (7, 9, 11‑13). The lipocalin structure of ApoM enables it to function as a carrier protein for small hydrophobic molecules including retinol (Vitamin A), all-trans-retinoic acid, 9-cis-retinoic acid, and sphingosine-1-phosphate (S1P) (14, 15). ApoM delivers S1P to S1P1 receptors and contributes to the maintenance of vascular endothelial integrity (15).

References

  1. Christoffersen, C. and L.B. Nielsen (2013) Curr. Opin. Lipidol. May 6 Epub. PMID 23652568.
  2. Arkensteijn, B.W. et al. (2013) Int. J. Mol. Sci. 14:4419.
  3. Xu, N. and B. Dahlback (1999) J. Biol. Chem. 274:31286.
  4. Zhang X.Y. et al. (2003) Acta Histochem. 105:67.
  5. Christoffersen, C. et al. (2008) J. Biol. Chem. 283:18765.
  6. Faber, K. et al. (2006) Mol. Endocrinol. 20:212.
  7. Christoffersen, C. et al. (2010) Circ. Res. 106:1624.
  8. Christoffersen, C. et al. (2012) J. Lipid Res. 53:2198.
  9. Christoffersen, C. et al. (2008) J. Biol. Chem. 283:1839.
  10. Christoffersen, C. et al. (2006) J. Lipid Res. 47:1833.
  11. Mulya, A. et al. (2010) J. Lipid Res. 51:514.
  12. Wolfrum, C. et al. (2005) Nat. Med. 11:418.
  13. Elsoe, S. et al. (2012) Atherosclerosis 221:91.
  14. Ahnstrom, J. et al. (2007) J. Lipid Res. 48:1754.
  15. Christoffersen, C. et al. (2011) Proc. Natl. Acad. Sci. USA 108:9613.

Alternate Names

APOM, NG20, Protein G3a

Entrez Gene IDs

55937 (Human); 55938 (Mouse); 55939 (Rat)

Gene Symbol

APOM

UniProt

Additional Apolipoprotein M/ApoM Products

Product Documents for Recombinant Human Apolipoprotein M Protein, CF

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Apolipoprotein M Protein, CF

For research use only

Related Research Areas

Citations for Recombinant Human Apolipoprotein M Protein, CF

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