|Other Names||Long-chain-fatty-acid--CoA ligase 4, Long-chain acyl-CoA synthetase 4, LACS 4, ACSL4, ACS4, FACL4, LACS4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2536b was selected from the Center region of human FACL4 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||ACS4, FACL4, LACS4|
|Function||Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses arachidonate and eicosapentaenoate as substrates.|
|Cellular Location||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|
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Provided below are standard protocols that you may find useful for product applications.
Long chain acyl-CoA synthetase (LACS), or long chain fatty acid-CoA ligase (FACL), converts free long chain fatty acids into fatty acyl-CoA esters, key intermediates in the synthesis of complex lipids. The FACL4 gene encodes a form of LACS and is expressed in several tissues, including brain. FACL4 cDNA from brain encodes a gene product that shows preference for arachidonic acid as a substrate when expressed in mammalian cells.1 The sequence of the predicted 670-amino acid human protein is 97% identical to that of rat ACS4. FACL4 is highly expressed in adult human brain, especially in the cerebellum and hippocampus, similar to the mouse.2 A strong cytoplasmic staining was found in the Purkinje and granular cells of the cerebellum and the pyramidal layer of hippocampus, indicating that FACL4 is specifically expressed in neurons and not in glial cells. Two patients with Alport syndrome, elliptocytosis, and mental retardation carried a large deletion of the COL4A5 region that included FACL4.3 The absence of FACL4 might play a role in the development of mental retardation or other signs associated with Alport syndrome. Two point mutations, 1 missense and 1 splice site change, were reported in the FACL4 gene in 2 families with nonspecific mental retardation.2 Analysis of enzymatic activity in lymphoblastoid cell lines of affected individuals revealed low levels compared with normal cells, indicating that both mutations are null mutations.
Mashek, D.G., et al., J. Lipid Res. 45(10):1958-1961 (2004).Sung, Y.K., et al., Cancer Sci. 94(5):421-424 (2003).Longo, I., et al., J. Med. Genet. 40(1):11-17 (2003).Meloni, I., et al., Nat. Genet. 30(4):436-440 (2002).Cao, Y., et al., Cancer Res. 61(23):8429-8434 (2001).
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