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Recombinant Human LDLR Protein (His Tag)
SKU: PKSH033435-50
Recombinant Human LDLR Protein (His Tag)
| SKU # | PKSH033435 |
| Expression Host | HEK293 Cells |
Description
| Synonyms | FH, FHC, LDL R, LDL Receptor, LDLCQ2, LDLR, Low-Density Lipoprotein Receptor |
| Species | Human |
| Expression Host | HEK293 Cells |
| Sequence | Ala22-Arg788 |
| Accession | P01130 |
| Calculated Molecular Weight | 86.56 kDa |
| Observed Molecular Weight | 99-135 kDa |
| Tag | C-His |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from a 0.2 μm filtered solution of 20mM HEPES, 150mM NaCl, pH 7.4. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
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).