LDLR Antibodies
Background
The LDLR gene encodes a low-density lipoprotein receptor, which is a transmembrane protein widely distributed on the surface of liver cells. Its main function is to maintain the balance of cholesterol metabolism by mediating the endocytosis of low-density lipoprotein (LDL) in plasma. This receptor can specifically recognize and bind to apolipoprotein B-100, internalize LDL particles into cells for degradation, thereby regulating blood cholesterol levels. Since its discovery by the team of Michael Brown and Joseph Goldstein in 1974, LDLR has become a key molecule in the study of cholesterol metabolism and atherosclerosis. The related research won the Nobel Prize in Physiology or Medicine in 1985. The in-depth interpretation of the function of LDLR not only reveals the pathogenesis of familial hypercholesterolemia, but also promotes the development of lipid-lowering therapies such as statins, laying a molecular foundation for the prevention and treatment of cardiovascular diseases.
Structure of LDLR
The low-density lipoprotein receptor encoded by the LDLR gene is a type I transmembrane protein with a molecular weight of approximately 160 kDa. The molecular weight of this protein varies among different species, mainly due to the variation in the number of repetitive sequences in its ligand-binding domain.
| Species | Human | Mouse | Hamster | Bovine | Rabbit |
| Molecular Weight (kDa) | 160 | 158 | 155 | 162 | 159 |
| Primary Structural Differences | Seven ligand binding repeats | Six ligand binding repeats | The ligand binding domain is relatively short | The repetitive sequence is highly conserved | High structural similarity to humans |
This receptor consists of five major domains: The ligand-binding domain at the N-terminal contains seven cysteine-rich repeat sequences, which are responsible for specifically recognizing apolipoprotein B-100; The homologous domain of epidermal growth factor precursors is involved in receptor recycling. O-linked sugar domains provide structural support; Transmembrane domains are anchored to the cell membrane; And the cytoplasmic domain at the C-terminal contains NPxY internalization signals, mediating the endocytosis process of reticin-coated pits.
Fig. 1 Schematic of full-length LDLR and its truncated mutants (ΔLBD, ΔEGF).1
Key structural properties of LDLR:
- Modular multi-domain configuration
- Cysteine-rich ligands bind repeat sequences
- Epidermal growth factor (EGF) precursor homeodomain
- Intracellular domain NPxY motifs
Functions of LDLR
The core function of the LDLR gene-encoded protein is to maintain cholesterol homeostasis, and its specific functions cover the following aspects:
| Function | Description |
| Cholesterol clearance | Mediating the endocytosis of low-density lipoprotein (LDL) in plasma to remove cholesterol from the blood is the key to regulating plasma cholesterol levels. |
| Intracellular internalization | The receptor-ligand complex is internalized into the cell by the reticin coating the fossa, achieving efficient uptake of LDL particles. |
| Receptor recycling | After LDL is released in an acidic endosome environment, the receptor can return to the cell membrane surface, achieving multiple cycles of reuse and enhancing the clearance efficiency. |
| Signal transduction regulation | By influencing intracellular cholesterol levels, it indirectly regulates cholesterol synthesis-related signaling pathways such as the SREBP pathway. |
| Prevention of atherosclerosis | The normal operation of its functions can effectively prevent abnormal deposition of cholesterol on the walls of blood vessels and reduce the risk of atherosclerosis. |
This receptor shows high affinity and saturation for LDL uptake, and its functional activity is strictly feedback inhibited by cellular cholesterol levels. This precise regulatory mechanism is crucial for maintaining the balance of lipid metabolism in the body.
Applications of LDLR and LDLR Antibody in Literature
1. Xu, Zhi-Sheng, et al. "LDLR is an entry receptor for Crimean-Congo hemorrhagic fever virus." Cell research 34.2 (2024): 140-150. https://doi.org/10.1038/s41422-023-00917-w
This study found that the low-density lipoprotein receptor (LDLR) is the key receptor for the Crimean-Congo hemorrhagic fever virus (CCHFV) to enter host cells. Viruses mediate infection through the binding of their glycoprotein Gc to LDLR. Blocking this receptor can significantly inhibit viral infection, providing a new strategy for the treatment of this disease.
2. Meshkov, Alexey, et al. "The LDLR, APOB, and PCSK9 variants of index patients with familial hypercholesterolemia in Russia." Genes 12.1 (2021): 66. https://doi.org/10.3390/genes12010066
Research has found that the low-density lipoprotein receptor (LDLR) is a key receptor for the Crimean-Congo hemorrhagic fever virus (CCHFV) to invade cells. Viruses bind to LDLR through their Gc proteins. Blocking this receptor can effectively inhibit infection, providing a new target for treatment.
3. Li, Zhelong, et al. "Exosome-based Ldlr gene therapy for familial hypercholesterolemia in a mouse model." Theranostics 11.6 (2021): 2953. https://www.thno.org/v11p2953.htm
Researchers successfully restored the expression of low-density lipoprotein receptors (LDLR) by delivering Ldlr mRNA to the livers of mice with LDLR gene deletion using exosomes. This therapy effectively reduced blood lipids and atherosclerotic plaques, providing a new strategy for the treatment of familial hypercholesterolemia (FH).
4. Yuan, Juanjuan, et al. "Correction to: Potentiating CD8+ T cell antitumor activity by inhibiting PCSK9 to promote LDLR-mediated TCR recycling and signaling." Protein & Cell 13.9 (2022): 694-700. https://doi.org/10.1007/s13238-021-00833-y
Research has found that low-density lipoprotein receptors (LDLR) play a key role in the anti-tumor activity of CD8+ T cells. It not only assists in cholesterol intake but also regulates the TCR cycle and signal transduction by interacting with the TCR complex. PCSK9 in the tumor microenvironment degrades LDLR, thereby inhibiting T cell function, which provides a new target for cancer immunotherapy.
5. Galicia-Garcia, Unai, et al. "Mutation type classification and pathogenicity assignment of sixteen missense variants located in the EGF-precursor homology domain of the LDLR." Scientific Reports 10.1 (2020): 1727. https://doi.org/10.1038/s41598-020-58734-9
This study focuses on the pathogenic gene LDLR of familial hypercholesterolemia (FH), and particularly analyzes 16 genetic variations in the homologous domain of its EGF precursor. The study classified these variations into non-pathogenic and pathogenic ones through functional experiments. The latter can be further divided into categories such as functional impairment, transport defect and recovery abnormality, providing an important basis for clinical diagnosis and treatment intensity.
Creative Biolabs: LDLR Antibodies for Research
Creative Biolabs specializes in the production of high-quality LDLR antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom LDLR Antibody Development: Tailor-made solutions to meet specific research requirements.
- Bulk Production: Large-scale antibody manufacturing for industry partners.
- Technical Support: Expert consultation for protocol optimization and troubleshooting.
- Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.
For more details on our LDLR antibodies, custom preparations, or technical support, contact us at email.
Reference
- Xu, Zhi-Sheng, et al. "LDLR is an entry receptor for Crimean-Congo hemorrhagic fever virus." Cell research 34.2 (2024): 140-150. https://doi.org/10.1038/s41422-023-00917-w
Anti-LDLR antibodies
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- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IGImmunochromatography
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot




