APOM Antibodies
Background
The APOM gene encodes apolipoprotein M, which is mainly present in high-density lipoprotein particles and participates in the lipid metabolic transport process as a member of the apolipoprotein family. The proteins it expresses can bind to bioactive lipids such as sphingosine phosphate, which not only promotes the stable transport of these lipids in the blood circulation but also regulates their biological activities in immune regulation and inflammatory responses. Studies have shown that APOM plays a significant role in maintaining retrograde cholesterol transport and endothelial function, and its abnormal expression is closely related to metabolic diseases such as atherosclerosis and diabetes. This gene was first identified through genomic sequencing in 2001. Its unique domain characteristics of lipocalciin provide an important model for understanding the mechanism of lipid-protein interactions and have key scientific value in revealing the functional diversity and metabolic regulatory network of high-density lipoproteins.
Structure of APOM
Apolipoprotein M encoded by the APOM gene is a protein with a molecular weight of approximately 21 kDa. Its weight varies among different species due to modifications such as glycosylation.
| Species | Human | Mouse | Rat |
| Molecular Weight (kDa) | ~21 | ~19 | ~20 |
| Primary Structural Differences | There is glycosylation modification | Highly homologous sequences, low degree of glycosylation | Similar to human APOM structure function |
This protein is composed of 188 amino acids, and its primary structure folds to form a typical lipid carrier protein domain. The three-dimensional structure of APOM contains a hydrophobic binding pocket, which can directly embed and carry bioactive lipids such as sphingosine phosphocholine. The binding ability of proteins to high-density lipoproteins stems from the anchoring of signal peptides at their N-terminal. Its tertiary structure mainly consists of eight anti-parallel β -folds forming a β -barrel, with the barrel mouth surrounded by an α -helix. The hydrophobic amino acid side chains inside the bucket form binding pockets, which form hydrogen bonds with the ligand heads through specific polar residues, thereby stabilizing lipids and regulating their biological activity.
Fig. 1 Schematic representation of human apoM in complex with S1P.1
Key structural properties of APOM:
- Lipid carrier protein folding structure
- Internal hydrophobic bonding cavity
- Apolipoprotein anchoring domain
Functions of APOM
The core function of the protein encoded by the APOM gene is to participate in lipid transport and metabolic regulation, and at the same time play an important role in immune regulation.
| Function | Description |
| Lipid transport | As a component of high-density lipoprotein, it is responsible for the transport and stability of bioactive lipids such as sphingosine and phosphocholine in the bloodstream. |
| Metabolic regulation | By forming pre-β -HDL particles and activating related signaling pathways, it promotes intracellular cholesterol efflux and maintains lipid metabolism balance. |
| Immune regulation | The sphingosine phosphocholine it carries can regulate lymphocyte migration and endothelial inflammatory responses, and affect the innate immune response. |
| Signal transduction | As a carrier, it will directionally deliver lipid signal molecules to specific tissues and participate in the regulation of processes such as cell proliferation and apoptosis. |
| Vascular protection | By maintaining the functional integrity of HDL, it inhibits the formation of atherosclerotic plaques and protects the function of endothelial cells. |
The binding curve of APOM to ligands shows the characteristic of specific high affinity, which is in line with its functional properties of precisely delivering signal lipids in complex metabolic environments.
Applications of APOM and APOM Antibody in Literature
1. Bisgaard, Line S., and Christina Christoffersen. "The apoM/S1P complex—a mediator in kidney biology and disease?." Frontiers in Medicine 8 (2021): 754490. https://doi.org/10.3389/fmed.2021.754490
The article indicates that apolipoprotein M and the sphingosinol-1-phosphate (S1P) it carries play an important role in renal physiology and diseases. The apoM/S1P axis is involved in regulating processes such as inflammation and endothelial permeability, and is closely related to acute and chronic kidney diseases. It is currently a highly promising drug target, but its specific mechanism still requires further research.
2. Mousa, Hanaa, Angelos Thanassoulas, and Susu M. Zughaier. "ApoM binds endotoxin contributing to neutralization and clearance by High Density Lipoprotein." Biochemistry and biophysics reports 34 (2023): 101445. https://doi.org/10.1016/j.bbrep.2023.101445
Studies have shown that apolipoprotein M (apoM) can bind endotoxin (LPS) with high affinity and assist HDL in neutralizing its toxicity, thereby inhibiting the release of inflammatory factors from macrophages. This reveals a key new mechanism of apoM in the anti-inflammatory function of HDL.
3. Stadler, Julia T., et al. "ApoM and Major Adverse Cardiovascular Events in Chronic Kidney Disease: A Prospective Cohort Study." Arteriosclerosis, Thrombosis, and Vascular Biology 45.4 (2025): 496-505. https://doi.org/10.1161/ATVBAHA.124.322367
Research has found that in patients with chronic kidney disease, the lower the level of plasma apolipoprotein M (APOM), the higher the risk of major adverse cardiovascular events and death. This indicates that APOM plays an important role in cardiovascular protection and is a potential risk indicator for it.
4. Hajny, Stefan, and Christina Christoffersen. "A novel perspective on the ApoM-S1P axis, highlighting the metabolism of ApoM and its role in liver fibrosis and neuroinflammation." International journal of molecular sciences 18.8 (2017): 1636. https://doi.org/10.3390/ijms18081636
Studies have found that apolipoprotein M (apoM) is expressed in the liver, kidney and blood-brain barriers, serving as a carrier of sphingosinol-1-phosphate (S1P). This review explores the novel role of the apoM-S1P axis in liver fibrosis, neuroinflammation and the integrity of the blood-brain barrier.
5. Bai Y, Pei W, et al. "ApoM is an important potential protective factor in the pathogenesis of primary liver cancer." Journal of Cancer 12.15 (2021): 4661. https://doi.org/10.7150/jca.53115
Studies have shown that apolipoprotein M (ApoM) plays a protective role in primary liver cancer. ApoM is lowly expressed in cancer tissues. Its absence promotes the proliferation, migration and invasion of liver cancer cells and accelerates tumorigenesis in mouse models, suggesting that ApoM is a potential tumor suppressor factor.
Creative Biolabs: APOM Antibodies for Research
Creative Biolabs specializes in the production of high-quality APOM antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom APOM 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 APOM antibodies, custom preparations, or technical support, contact us at email.
Reference
- Hajny, Stefan, and Christina Christoffersen. "A novel perspective on the ApoM-S1P axis, highlighting the metabolism of ApoM and its role in liver fibrosis and neuroinflammation." International journal of molecular sciences 18.8 (2017): 1636. https://doi.org/10.3390/ijms18081636
Anti-APOM 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




