Recombinant Human Apolipoprotein E/ApoE-kyoto Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Human Apolipoprotein E/ApoE-kyoto binds to Recombinant Human VLDLR Protein (Catalog #
8444-VL) with an ED 50 of 0.0500‑0.500 μg/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human Apolipoprotein E/ApoE protein Lys19-His318, Arg 43 Cys |
| Accession # |
|
| N-terminal Sequence |
Lys19 |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>90%, 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 |
34-40 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 |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Reconstitution Instructions |
Reconstitute at 100 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 E/ApoE-kyoto 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]. ApoE2-Kyoto (Cys25/Cys112/Arg158), a
rare variant of ApoE2, has been linked to lipoprotein glomerulopathy and
demonstrates altered receptor-binding and lipid-handling properties [6].
-
Zhang, X. et al. (2023) Cells
12:410.
- Horn, J.V.C. et al. (2023) Mol
Cell Biochem 478:173.
- Murphy, K.B. et al. (2025) Nat Commun 16:4883.
- Mahley, R.W. et al. (2012) J Lipid Res 53:539.
- Liu, C.C. et al. (2013) Nat Rev Neurol 9:106.
- Matsunaga, A. et al. (1999) Kidney International 56:421.
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