Recombinant Human Apolipoprotein E3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Human Apolipoprotein E3 Protein, CF Summary

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

When Recombinant Human Apolipoprotein E3/ApoE3 is immobilized at 1 μg/mL (100 μL/well), the concentration of recombinant mouse VLDL R that produces 50% of the optimal binding response is found to be approximately 0.075 ‑ 0.375 μg/mL.

Source
E. coli-derived human Apolipoprotein E3/ApoE3 protein
Lys19-His317, with an N-terminal Met and 6-His tag
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Gene
APOE
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

Theoretical MW
35.2 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.
Publications
Read Publications using
4144-AE 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, -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MOPS, NaCl, CHAPS and TCEP.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Notes

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

Alternate Names for Recombinant Human Apolipoprotein E3 Protein, CF

  • AD2
  • Apo-E
  • ApoE4
  • apolipoprotein E
  • Apolipoprotein E3
  • LDLCQ5
  • LPG

Background

ApoE is a major protein component of serum LDL, VLDL, HDL, and chylomicrons. It is produced predominantly by hepatocytes, macrophages, and non-neuronal cells in the CNS. ApoE-containing particles transport triglycerides and cholesterol to peripheral tissues for cellular uptake and catabolism (1 - 4). Mature human ApoE is a 34 kDa glycoprotein that consists of an N-terminal domain composed of four bundled alpha -helices, plus a hinge region and an extended alpha -helical C-terminal domain (2, 5). Its amphipathic nature and flexible structure enables it to adopt dramatically different conformations upon lipid association (2). ApoE is monomeric in lipid particles, although it forms oligomers when lipid-free (6). ApoE3 is the most abundant of the three common alleles in human; ApoE2 and ApoE4 differ by single aa substitutions (1). Mature human ApoE shares 71% aa sequence identity with mouse and rat ApoE. LDL receptor family proteins preferentially bind and internalize the lipid-bound form of ApoE with the exception of VLDLR which also efficiently internalizes lipid-free ApoE (7, 8). Lipoprotein uptake is facilitated by the initial binding of ApoE to cell surface heparan sulfate proteoglycans (HSPG) (9). Receptor/HSPG binding and lipid interactions primarily involve the N- and C-terminal regions of ApoE, respectively (2). Recycled lipid-free ApoE is formed into HDL particles through interactions with the lipid transporter ABCA1 (10). High cellular sterol content activates the nuclear hormone receptor LXR which promotes increased ApoE synthesis and increased sterol efflux, while low sterol content induces LDL R expression with increased sterol uptake and decreased ApoE production (11). ApoE3 dampens the TNF-alpha induced inflammatory response in vascular endothelial cells (12). In the CNS, ApoE blocks production of the amyloid A beta peptide by inhibiting the gamma -secretase cleavage of APP (13). It also complexes with A beta and promotes A beta internalization via LRP2 (14, 15).

  1. Martins, I.J. et al. (2006) Mol. Pschiatry 11:721.
  2. Hatters, D.M. et al. (2006) Trends Biochem. Sci. 31:445.
  3. Heeren, J. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26:442.
  4. Mahley, R.W. et al. (1984) J. Lipid. Res. 25:1277.
  5. Zannis, V.I. et al. (1984) J. Biol. Chem. 259:5495.
  6. Perugini, M.A. et al. (2000) J. Biol. Chem. 275:36758.
  7. Ruiz, J. et al. (2005) J. Lipid Res. 46:1721.
  8. Chroni, A. et al. (2005) Biochemistry 44:13132.
  9. Futamura, M. et al. (2005) J. Biol. Chem. 280:5414.
  10. Krimbou, L. et al. (2004) J. Lipid. Res. 45:839.
  11. Lucic, D. et al. (2007) J. Lipid Res. 48:366.
  12. Mullick, A.E. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:339.
  13. Irizarry, M.C. et al. (2004) J. Neurochem. 90:1132.
  14. Naslund, J. et al. (1995) Neuron 15:219.
  15. Zerbinatti, C.V. et al. (2006) J. Biol. Chem. 281:36180.

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Publications for Apolipoprotein E3/ApoE3 (4144-AE)(4)

We have publications tested in 3 confirmed species: Human, Mouse, Rat.

We have publications tested in 2 applications: Bioassay, Functional ELISA.


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Bioassay
(3)
Functional ELISA
(1)
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Human
(1)
Mouse
(2)
Rat
(1)
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Bioinformatics

Gene Symbol APOE
Entrez
Uniprot