Human ApoE4
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| Cat-Nr. | 100-126S |
| Size | 100 µg |
| Price | 95 € |
| Source | E. coli |
| Formulation | lyophilized |
| Purity Confirmation | > 95% by SDS-PAGE & Coomassie stain |
| Length [aa] | 300 |
| Molecular Weight | 34.4 kDa |
| N Terminal Sequence | MEVEQA |
| Biological Activity | Data not available. |
| Species Reactivity | Human |
| Buffer | PBS |
| Synonyms | APOE; AD2; LPG; LDLCQ5 |
| Description | ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues. |
| Protein Sequence | MKVEQAVETE PEPELRQQTE WQSGQRWELA LGRFWDYLRW VQTLSEQVQE ELLSSQVTQE LRALMDETMK ELKAYKSELE EQLTPVAEET RARLSKELQA AQARLGADME DVRGRLVQYR GEVQAMLGQS TEELRVRLAS HLRKLRKRLL RDADDLQKRL AVYQAGAREG AERGLSAIRE RLGPLVEQGR VRAATVGSLA GQPLQERAQA WGERLRARME EMGSRTRDRL DEVKEQVAEV RAKLEEQAQQ IRLQAEAFQA RLKSWFEPLV EDMQRQWAGL VEKVQAAVGT SAAPVPSDNH |
| Uniprot ID | P02649 |
| Protein RefSeq | NP_000032.1 |
| mRNA RefSeq | NM_000041.2 |
Figures
SDS-PAGE analysis of recombinant human ApoE4. Sample (1µg/lane) was loaded in 18% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.
Reference
- Apolipoprotein E4 Elicits Lysosomal Cathepsin D Release, Decreased Thioredoxin-1 Levels, and Apoptosis. T. Persson et al., J Alzheimers Dis. 2017; 56(2): 601–617.
- Thioredoxin-80 is a product of alpha-secretase cleavage that inhibits amyloid-beta aggregation and is decreased in Alzheimer's disease brain. F. Gil-Bea et al., EMBO Mol Med. 2012 Oct; 4(10): 1097–1111.
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