Recombinant Human Apolipoprotein E4/ApoE4 Protein, CF Summary
| Additional Information |
HEK Expressed |
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Human Apolipoprotein E4/ApoE4 binds to Recombinant Human VLDLR Protein (Catalog #
8444-VL) with an ED 50 of 10.0‑100 ng/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human Apolipoprotein E4/ApoE4 protein Lys19-His318 |
| Accession # |
|
| N-terminal Sequence |
Lys 19 |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
34 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 |
32-39 kDa, under reducing conditions. |
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 MOPS, NaCl and TCEP with Trehalose. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 250 μg/mL in water. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Apolipoprotein E4/ApoE4 Protein, CF
Background
Apolipoprotein
E (ApoE) is a polymorphic lipid-transport protein with three major human
isoforms-ApoE2, ApoE3, and ApoE4-differing by single amino acid substitutions
at residues 112 and 158, which significantly alter their structure and function
[1, 2]. All isoforms share a two-domain
structure: the N-terminal domain mediates receptor binding, while the
C-terminal domain facilitates lipid binding and oligomerization [2]. ApoE3
(Cys112/Arg158) is the most common and functionally neutral isoform, while
ApoE2 (Cys112/Cys158) has reduced affinity for LDL receptors, often leading to
type III hyperlipoproteinemia in homozygotes [1, 4]. ApoE4 (Arg112/Arg158)
exhibits a more compact and less stable structure due to domain interaction,
predisposing it to pathological effects in the brain [2, 5]. Functionally, ApoE
isoforms differentially regulate neuronal metabolism: ApoE2 enhances glycolytic
activity and hexokinase expression, promoting neuroprotection, whereas ApoE4
impairs these pathways, increasing vulnerability to aging and Alzheimer's
disease (AD) [1]. Recent transcriptomic and epigenomic profiling of human
microglia in an AD xenotransplantation model revealed that ApoE isoforms
distinctly shape gene expression and chromatin accessibility. ApoE4 drives
pro-inflammatory and neurodegenerative signatures, while ApoE2 supports
homeostatic microglial states [3]. Clinically, ApoE genotyping is widely used
to assess AD risk, with ApoE4 being the strongest genetic risk factor and ApoE2
offering relative protection [4, 5]. Therapeutic strategies targeting ApoE
include isoform-specific modulation and gene editing. Additionally, ApoE
isoforms are valuable tools in translational research for drug screening,
biomarker discovery, and personalized medicine [4].
-
Zhang
X, et al. (2023) Cells
12:410.
- Horn
JVC, et al. (2023) Mol
Cell Biochem 478: 173.
- Murphy
KB, et al. (2025) Nat Commun 16:4883.
- Mahley
RW, et al. (2012) J Lipid Res 53:539.
- Liu
CC, et al. (2013) Nat Rev Neurol 9:106.
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