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Gibco™ Human ApoE4 Recombinant Protein, PeproTech® DFS Item

Recombinant Protein

Supplier:  Gibco™ LS35004100UG

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Numéro de catalogue. 35004100UG


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Description

Description

350-04-1MG will be provided as 2 x 500 μg (350-04-500UG). Recombinant Human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues. This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization 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 the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. 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.
Spécifications

Spécifications

P02649
protein with no preservative
34.4 kDa
100 μg
RUO
APO-E; Apolipoprotein E3
APOE
Recombinant
-20°C
Lyophilized
Functional Assay
348
Human ApoE4
E. coli
<1 EU/ μg
ApoE4
Unconjugated
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
E. coli
≥ 90% by SDS-PAGE gel and HPLC analyses.
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