LDLR, FLAG-Avi-Tag, Biotin-Labeled Recombinant
CAT:
421-71206-2
Size:
50 µg
Price:
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- Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
- Dry Ice Shipment: Yes


LDLR, FLAG-Avi-Tag, Biotin-Labeled Recombinant
Background:
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. In case of HIV-1 infection, it functions as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells. PCSK9 binds to the epidermal growth factor-like repeat A (EGF-A) domain of LDLR, inducing LDLR degradation.Description:
Recombinant human LDLR (Low Density Lipoprotein Receptor), encompassing amino acids 22-788. This construct contains a C-terminal FLAG-tag followed by an Avi-Tag™. The recombinant protein was enzymatically biotinylated using the Avi-Tag™ and affinity purified.UniProt:
P01130Tag:
C-terminal FLAG and Avi tagsLabel:
This protein is enzymatically biotinylated using Avi-Tag™ technology. Biotinylation is confirmed to be >90%.For more information on enzymatic biotinylation, please see ourTech Note.Applications:
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.Purity:
≥ 90%Format:
Aqueous buffer solutionShipping Conditions:
-80°CStorage Conditions:
At least 6 months at -80°C.Calculated Molecular Weight:
88 kDa + glycansFormulation:
8 mM phosphate, pH 7.4,110 mM NaCl, 2.2 mM KCl, and 20% glycerolGlycosylation:
This protein runs at a higher MW by SDS-PAGE due to glycosylation.