Product Information
| Property | Description |
| Product Name | Anti-human LXRα Recombinant Monoclonal Antibody |
| Antibody ID | HM0023 |
| Target Protein | Oxysterols receptor LXR-alpha (LXRα / NR1H3) |
| UniProt Accession | Q13133-1 / Q13133-2 |
| Molecular Weight | Isoform 1: 50.4 kDa; Isoform 2: 43.6 kDa |
| Antibody Type | Recombinant monoclonal antibody |
| Host Species | Mouse |
| Recombinant Format | Full-length mouse IgG1 |
| Isotype | Mouse IgG1 |
| Species Reactivity | Human validated only |
| Tested Applications | WB, ELISA |
| Recommended Dilution for WB | 1:500–1:5000 |
| Antigen | Human-derived recombinant epitope-Fc fusion protein |
| Epitope Sequence | DIPPDSAVELWKPGAQDASSQA |
| Expression System | HEK293 cells |
| Purification | Protein G affinity chromatography |
| Conjugate | Unconjugated |
| Concentration | 0.1 mg/mL |
| Storage Buffer | 0.1 M Tris, 0.05 M Glycine, 0.07 M NaCl, 2 g/L BSA, 50% glycerol, pH 7 |
| Storage Condition | Store at -20°C |
| Research Use | For research use only. Not for diagnostic or therapeutic applications. |
Product Background
Liver X receptor alpha (LXRα, NR1H3) is a ligand-activated nuclear receptor involved in cholesterol metabolism, lipid homeostasis, inflammatory signaling, and metabolic regulation. Human LXRα is widely studied in liver biology, cardiovascular disease, lipid metabolism, and inflammatory signaling pathways. Due to its important role in cholesterol transport and metabolic regulation, LXRα is an important target in metabolism and translational research.
Also known as: hLXRa, hLXRα, Human LXRa, Human LXRα, Human LXR alpha, LXRa, LXRα, LXR alpha, Liver X receptor alpha, Liver X receptor-alpha, Oxysterols receptor LXR-alpha, Oxysterols receptor alpha, and NR1H3.
Antibody Development
HM0023 was generated by phage-display selection using a mouse-derived antibody library. A human-derived recombinant epitope-Fc fusion protein containing the LXRα epitope sequence was used as the selection antigen. Following identification of the initial antibody candidate, structure-guided affinity optimization was performed to improve binding affinity and specificity.
The optimized antibody was reconstructed as a full-length mouse IgG1 recombinant antibody and expressed in HEK293 cells.
Binding and specificity were evaluated by:
- ELISA using human-derived recombinant epitope-Fc fusion antigen
- Western blot using recombinant MBP-epitope fusion protein
- Western blot detection of endogenous human LXRα protein in mammalian cell lysates
Validation Data
ELISA Validation
ELISA demonstrated specific binding to the human-derived recombinant epitope-Fc fusion antigen, while minimal binding was observed against Fc control protein.
Validation conditions:
- Well 1: Fc control protein
- Well 2: Epitope-Fc fusion protein
- Detection substrate: TMB
Note: ELISA validation confirms binding to the epitope-Fc fusion antigen. Full-length LXRα protein binding in solution has not been tested by ELISA.
Western Blot Validation – Recombinant Fusion Protein
Western blot analysis demonstrated specific recognition of recombinant MBP-epitope fusion protein expressed in BL21(DE3) cells, while no significant binding was observed against MBP control protein.
Validation conditions:
- Lane 1: MBP control protein
- Lane 2: MBP-epitope fusion protein
- Standard reducing Western blot
Western Blot Validation – Endogenous Full-Length Protein
Western blot analysis detected endogenous human LXRα protein in mammalian tissue and cell lysates under reducing conditions.
Validated samples:
- HEK293T cells
- HeLa cells
- HepG2 cells
Detection condition:
- Standard reducing Western blot
- HRP-conjugated anti-mouse secondary antibody















