Recombinant Human LDL Receptor protein (Tagged) (ab271587)
Key features and details
- Expression system: HEK 293 cells
- Purity: >= 90% SDS-PAGE
- Tags: DDDDK tag C-Terminus
- Suitable for: SDS-PAGE
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Product name
Recombinant Human LDL Receptor protein (Tagged)
See all LDL Receptor proteins and peptides -
Purity
>= 90 % SDS-PAGE. -
Expression system
HEK 293 cells -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Predicted molecular weight
86 kDa -
Amino acids
22 to 788 -
Tags
DDDDK tag C-Terminus -
Additional sequence information
Extracellular domain. Eu-labeled.
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Preparation and Storage
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Alternative names
- FH
- FHC
- LDL R
see all -
Function
Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. In case of HIV-1 infection, functions as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. -
Involvement in disease
Defects in LDLR are the cause of familial hypercholesterolemia (FH) [MIM:143890]; a common autosomal semi-dominant disease that affects about 1 in 500 individuals. The receptor defect impairs the catabolism of LDL, and the resultant elevation in plasma LDL-cholesterol promotes deposition of cholesterol in the skin (xanthelasma), tendons (xanthomas), and coronary arteries (atherosclerosis). -
Sequence similarities
Belongs to the LDLR family.
Contains 3 EGF-like domains.
Contains 7 LDL-receptor class A domains.
Contains 6 LDL-receptor class B repeats. -
Post-translational
modificationsN- and O-glycosylated.
Ubiquitinated by MYLIP leading to degradation. -
Cellular localization
Cell membrane. Endomembrane system. Membrane > clathrin-coated pit. Found distributed from the plasma membrane to intracellular compartments. - Information by UniProt
Images
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SDS-PAGE - Recombinant Human LDL Receptor protein (Tagged) (ab271587)
SDS-PAGE analysis of ab271587.
LDL Receptor is heavily glycosylated, resulting in higher molecular weight. The two bands shown correspond to differing states of glycosylation.