Low-Density Lipoprotein Receptor Active Protein | LDLR active protein

Recombinant Human Low-Density Lipoprotein Receptor Protein

Cat. Num. AAA2556728

• Gene Names: LDLR; FH; FHC; LDLCQ2
• Purity: >95% as determined by reducing SDS-PAGE.
• Synonyms: Low-Density Lipoprotein Receptor; Recombinant Human Low-Density Lipoprotein Receptor Protein; LDL Receptor; LDLR; LDLR active protein

• Host: Human Cells
• Purity/Purification: >95% as determined by reducing SDS-PAGE.
• Form/Format: Lyophilized from a 0.2 mum filtered solution of 50mM HEPES, 150mM NaCl, pH 7.4.
• Sequence Length: 860

• Species: Human
• Endotoxin: <1.0 EU per ug as determined by LAL test.
• Fragment: Ala22-Arg788
• Fusion Tag: C-6His
• Activity: Measure by its ability to bind with human PCSK9 in a functional ELISA.Immobilized human PCSK9 at 10 mug/ml (100 mul/well) can bind biotinylated recombinant human LDLR. The EC50 of biotinylated human LDLR is 0.61 mug/ml. 2. Immobilized mouse PCSK9 at 10 mug/ml (100 mul/well) can bind biotinylated recombinant human LDLR. The EC50 of biotinylated human LDLR is 0.12 mug/ml.
• Preparation and Storage: Lyophilized protein should be stored at < -20 degree C, though stable at room temperature for 3 weeks.; Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days.; Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.

SDS-Page

Related Product Information for LDLR active protein

Protein Construction: Recombinant Human Low-Density Lipoprotein Receptor is produced by our Mammalian expression system and the target gene encoding Ala22-Arg788 is expressed with a 6His tag at the C-terminus.

Background: Low-Density Lipoprotein Receptor (LDLR) is a transmembrane glycoprotein that plays a critical role in cholesterol homeostasis. LDLR mediates blood cholesterol level by interacting with lipoprotein particles like LDL and VLDL. The extracellular domain of LDLR contains LDL receptor type A (ligand-binding) modules (LA repeats), epidermal growth factor-like modules, and LY repeats containing the YWTD consensus motif that are important in binding and releasing of ApoB-100 and ApoE in lipoprotein particles. The C terminal domain of LDLR inside the cell is required for the receptor internalization. Loss of function mutations in the LDLR gene causes Familial Hypercholesterolemia (FH).

NCBI and Uniprot Product Information

• NCBI GI #: 4504975
• NCBI GeneID: 3949
• NCBI Accession #: NP_000518.1
• NCBI GenBank Nucleotide #: NM_000527.4
• UniProt Accession #: P01130; Q53ZD9; Q59FQ1; Q9UDH7; B4DII3; B4DJZ8; B4DR00; B4DTQ3; C0JYY8; H0YLU8; H0YNT7
• Molecular Weight: Molecular Mass: 84.8kDa; Actual Protein Molecular Mass: 99-135kDa
• NCBI Official Full Name: low-density lipoprotein receptor isoform 1
• NCBI Official Synonym Full Names: low density lipoprotein receptor
• NCBI Official Symbol: LDLR
• NCBI Official Synonym Symbols: FH; FHC; LDLCQ2
• NCBI Protein Information: low-density lipoprotein receptor
• UniProt Protein Name: Low-density lipoprotein receptor
• Protein Family: Low-density lipoprotein receptor
• UniProt Gene Name: LDLR
• UniProt Synonym Gene Names: LDL receptor

NCBI Description

The low density lipoprotein receptor (LDLR) gene family consists of cell surface proteins involved in receptor-mediated endocytosis of specific ligands. Low density lipoprotein (LDL) is normally bound at the cell membrane and taken into the cell ending up in lysosomes where the protein is degraded and the cholesterol is made available for repression of microsomal enzyme 3-hydroxy-3-methylglutaryl coenzyme A (HMG CoA) reductase, the rate-limiting step in cholesterol synthesis. At the same time, a reciprocal stimulation of cholesterol ester synthesis takes place. Mutations in this gene cause the autosomal dominant disorder, familial hypercholesterolemia. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Sep 2010]

Uniprot Description

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.