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. 2014 Dec 9;9(12):e114877. doi: 10.1371/journal.pone.0114877

Figure 1. Alignment of FACL6 amino acid sequence with eukaryotic FATPs and purification of FACL6.

Figure 1

A, The FACL6 (Rv1206) amino acid sequence was aligned with human FATP1 (HsFATP1), human FATP4 (HsFATP4) and yeast FATP (ScFAT) amino acid sequences using the ClustalW2 multiple sequence alignment program. Amino acid identities are shaded in black and similarities shaded in gray. The diagonally hatched boxes above the amino acid sequences indicate the location of the AMP-binding domain and the vertically hatched boxes indicate the location of the very long-chain acyl-CoA synthetase (VLACS) domain on the human FATP1. The peptide indicated by a box and arrow at the C-terminal end of Rv1206 (FACL6) was used to raise a polyclonal antiserum against FACL6. B, Purification of FACL6 expressed in E. coli. The FACL6 protein was solubilized and affinity-purified as described in Materials and Methods. Coomassie-stained denaturing polyacrylamide gel shown. Lanes: 1 and 5, molecular weight standards (sizes indicated on left); 2, cell lysate; 3, 16,000×g supernatant; 4, supernatant from solubilized 16,000 x g pellet; 6, column flow-through; 7 and 8, column wash; 9 and 10, eluted fractions containing purified FACL6 protein.