Anti-ELOVL4 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

ELOVL4 or Elongation of Very Long Chain Fatty Acids Protein 4 plays a critical role in the biosynthesis of very long chain fatty acids. It weighs approximately 32 kDa. It elongates saturated and polyunsaturated fatty acids extending carbon chains to lengths exceeding 24 carbons. ELOVL4 is found mainly in the retina skin and brain reflecting its significance in these tissues. Its mechanical function involves adding two carbons per cycle to endogenous and dietary fatty acids substrates.

Biological function summary

This enzyme contributes to the production of essential lipids that maintain cellular structure and function. ELOVL4 integrates into larger protein complexes that regulate its activity or stabilize its function. It influences the quality of long-chain ceramides and other sphingolipids which impact barrier functions particularly in the skin and retina. Moreover it participates in maintaining membrane integrity and dynamics where these specialized lipids concentrate.

Pathways

ELOVL4 participates prominently in sphingolipid and lipid metabolism pathways. It interacts with other elongases and desaturases such as ELOVL1 to execute its elongation tasks. This protein's activity bears importance in both the synthesis and modification phases of very long-chain fatty acids critical to cellular processes. The sphingolipid pathway necessitates ELOVL4 in producing functional lipids ensuring proper membrane properties and signaling events.

Associated diseases and disorders

Mutations in the ELOVL4 gene have links to conditions like Stargardt-like macular dystrophy and ichthyosis. Stargardt disease involves retinal degeneration due to disruptions in photoreceptor cell function attributed to defective fatty acid elongation. In skin-related disorders like ichthyosis ELOVL4 mutations disturb lipid processing affecting skin barrier formation. Pathologically its dysfunction associates with other lipogenic and barrier-forming proteins including ceramide synthases impacting the synthesis of necessary lipid components.