Recombinant Human LDL Receptor protein (Tagged) is a Human Fragment protein, in the 22 to 788 aa range, expressed in HEK 293, with >=90% purity and suitable for SDS-PAGE.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Binds low density lipoprotein /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. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization (PubMed:30443021). (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins. (Microbial infection) Acts as a receptor for Vesicular stomatitis virus. (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. (Microbial infection) Acts as a receptor for Crimean-Congo hemorrhagic fever virus (CCHFV). (Microbial infection) Acts as a receptor for many Alphavirus, including Getah virus (GETV), Ross river virus (RRV) and Semliki Forest virus.
Low-density lipoprotein receptor, LDL receptor, LDLR
Recombinant Human LDL Receptor protein (Tagged) is a Human Fragment protein, in the 22 to 788 aa range, expressed in HEK 293, with >=90% purity and suitable for SDS-PAGE.
pH: 7.4
Constituents: PBS, 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.13% Sodium phosphate, 0.02% Potassium chloride
Binds low density lipoprotein /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. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization (PubMed:30443021).
Belongs to the LDLR family.
N- and O-glycosylated.
The LDL Receptor also called LDLR is a protein that plays an important role in the uptake and clearance of low-density lipoproteins (LDL) from the bloodstream. LDLR binds LDL particles facilitating their internalization through receptor-mediated endocytosis. This receptor is expressed mainly in the liver adrenal glands and other tissues involved in cholesterol metabolism. It has an approximate molecular weight of 160 kDa. Researchers often study LDLR using techniques like Western blotting to understand its presence and function.
The LDL receptor interacts with LDL particles to regulate cholesterol levels in the body. It is part of a cell surface complex that recognizes and binds to apolipoprotein B-100 or apolipoprotein E present on LDL. This interaction initiates internalization of LDL leading to its degradation in lysosomes where cholesterol can be released and used by the cell. Mutations in the gene encoding LDLR can lead to inefficient cholesterol uptake influencing various metabolic processes.
LDL receptor activities are integral to lipid metabolism and cholesterol homeostasis. Two important biological pathways that involve LDLR include the cholesterol biosynthesis pathway and the lipoprotein clearance pathway. Within these pathways LDLR collaborates closely with proteins like PCSK9 which modulates its expression and degradation and HMG-CoA reductase an important enzyme in cholesterol synthesis to balance cholesterol levels in the body.
Defects in the LDL receptor are strongly associated with familial hypercholesterolemia and atherosclerosis. These conditions arise from impaired clearance of LDL leading to elevated cholesterol levels which pose risks for cardiovascular diseases. LDLR dysfunctions are linked with the Protein PCSK9 whose gain-of-function mutations can exacerbate hypercholesterolemia by promoting degradation of LDLR while statins aim to increase LDLR expression to lower LDL cholesterol levels.
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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.
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