Anti-ACSL3 Antibody Picoband® Fluoro488 Conjugated

Long-chain-fatty-acid—CoA ligase 3 is an enzyme that in humans is encoded by the ACSL3 gene. The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene.

E.coli-derived human ACSL3 recombinant protein (Position: M12-I224) . Human ACSL3 shares 91.1% and 90.1% amino acid (aa) sequence identity with mouse and rat ACSL3, respectively.

Expressed in breast, ductal and invasive ductal carcinomas of the breast, sporadic colorectal adenomas and carcinomas (at protein level) . Expressed in fetal brain. Expressed in lung, amygdala, eye, prostate, pancreatic and prostate cancers, head and neck tumors and embryonal tumor.

Cardiovascular, Fatty Acid Oxidation, Fatty Acids, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Redox Metabolism, Signal Transduction

Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity) . Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity) . Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) . .

1. Entrez Gene: ACSL3 acyl-CoA synthetase long-chain family member 3. 2. Bakken AM, Farstad M, Holmsen H (Feb 1991) .Identity between palmitoyl-CoA synthetase and arachidonoyl-CoA synthetase in human platelet?.The Biochemical Journal. 274 (Pt 1) (1) : 145–52. 3. Minekura H, Kang MJ, Inagaki Y, Suzuki H, Sato H, Fujino T, Yamamoto TT (Oct 2001) . Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. Gene. 278 (1-2) : 185–192.

Mitochondrion outer membrane ; Single-pass type III membrane protein . Peroxisome membrane ; Single-pass type III membrane protein . Microsome membrane ; Single-pass type III membrane protein . Endoplasmic reticulum membrane ; Single-pass type III membrane protein .