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Long-chain acyl-CoA synthetase 4 (ACSL4) is a CoA ligase and member of the ACSL family.1,2 It is composed of an N-terminal membrane-binding domain, a transmembrane domain, an adenosine adaptor region, and a C-terminal catalytic domain.2 ACSL4 is primarily found in the mitochondria, peroxisomes, endoplasmic reticulum (ER), and plasma membrane.1,3 It is generally involved in fatty acid degradation via β-oxidation and lipid synthesis.2 Specifically, ACSL4 ligates 20-chain PUFAs, such as eicosapentaenoic acid (Item Nos. 90110 | 90110.1 | 21908) or arachidonic acid (Item Nos. 90010 | 90010.1 | 10006607), to CoA to form fatty acyl-CoA esters, which are then used for lipid synthesis, plasma membrane repair, and as a carbon source in the citric acid cycle, among other processes.2,4 However, this process can be dysregulated by increased intracellular levels of ferrous iron (Fe2+) and reactive oxygen species (ROS) that further oxidize these PUFA fatty acyl-CoA esters into lipid peroxides that contribute to the development of ferroptosis.3,5,6 Increased expression of ACSL4 is associated with higher cancer staging in patients with prostate cancer.7 Cayman's ACSL4 (42-711) (human, recombinant) protein can be used for enzyme activity, ELISA, and Western blot (WB) applications.
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1. ACSL family: The regulatory mechanisms and therapeutic implications in cancer. Eur. J. Pharmacol. 909, 174397 (2021).
2. The ACSL4 network regulates cell death and autophagy in diseases. Biology (Basel) 12(6), 864 (2023).
3. ACSL3 and ACSL4, distinct roles in ferroptosis and cancers. Cancers (Basel) 14(23), 5896 (2022).
4. Reactive acyl-
5. CD8+ T cells and fatty acids orchestrate tumor ferroptosis and immunity via ACSL4. Cancer Cell 40(4), 365-378 (2022).
6. PKCβII phosphorylates ACSL4 to amplify lipid peroxidation to induce ferroptosis. Nat. Cell Biol. 24(1), 88-98 (2022).
7. ACSL4 promotes prostate cancer growth, invasion and hormonal resistance. Oncotarget 6(42), 44849-44863 (2015).