ACSL4 (42-711) (human, recombinant)

Long-chain acyl-CoA synthetase 4 (ACSL4) is a CoA ligase and member of the ACSL family. It is composed of an N-terminal membrane-binding domain, a transmembrane domain, an adenosine adaptor region, and a C-terminal catalytic domain. ACSL4 is primarily found in the mitochondria, peroxisomes, endoplasmic reticulum (ER), and plasma membrane. It is generally involved in fatty acid degradation via beta-oxidation and lipid synthesis. Specifically, ACSL4 ligates 20-chain PUFAs, such as eicosapentaenoic acid (Cay-90110, Cay-90110., Cay-21908) or arachidonic acid (Cay-90010, Cay-90010., Cay-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. 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. Increased expression of ACSL4 is associated with higher cancer staging in patients with prostate cancer. Cayman's ACSL4 (42-711) (human, recombinant) protein can be used for enzyme activity, ELISA, and Western blot (WB) applications. Protein Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590) [The Uniprot Consortium]