Purified by antigen-specific affinity chromatography.
Immunogen
Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human FACL3(long-chain fatty-acid-Coenzyme A ligase 3)
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
-20 °C
Minekura, Kang, Inagaki, Suzuki, Sato, Fujino, Yamamoto: "Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene." in: Gene, Vol. 278, Issue 1-2, pp. 185-92, (2001) (PubMed).
Minekura, Fujino, Kang, Fujita, Endo, Yamamoto: "Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35." in: Genomics, Vol. 42, Issue 1, pp. 180-1, (1997) (PubMed).
Fujino, Kang, Suzuki, Iijima, Yamamoto: "Molecular characterization and expression of rat acyl-CoA synthetase 3." in: The Journal of biological chemistry, Vol. 271, Issue 28, pp. 16748-52, (1996) (PubMed).
Rose, King, Summers, Palmer, Yang, Wilkie, Reardon, Malcolm, Winter: "Localization of the genetic locus for Saethre-Chotzen syndrome to a 6 cM region of chromosome 7 using four cases with apparently balanced translocations at 7p21.2." in: Human molecular genetics, Vol. 3, Issue 8, pp. 1405-8, (1995) (PubMed).
Brueton, van Herwerden, Chotai, Winter: "The mapping of a gene for craniosynostosis: evidence for linkage of the Saethre-Chotzen syndrome to distal chromosome 7p." in: Journal of medical genetics, Vol. 29, Issue 10, pp. 681-5, (1992) (PubMed).
Target
Acsl3
(Acyl-CoA Synthetase Long-Chain Family Member 3 (Acsl3))
The FACL3(long-chain fatty-acid-Coenzyme A ligase 3) 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.