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. Author manuscript; available in PMC: 2009 Aug 1.

Published in final edited form as: Biochim Biophys Acta. 2008 May 15;1781(8):359–366. doi: 10.1016/j.bbalip.2008.04.017

Fig. 2 — Fig. 2A. 3-ketoreductase sequence alignment with Erg27p internal deletions indicated as boxed areas. Homology plot of from Saccharomyces cerevisiae (top), Candida glabrata, Kluyvermyces lactis, Candida albicans, Mus musculus, Homo sapiens (bottom). Regions selected for internal deletions are outlined in red. Region 1 deleted amino acids 32–43 (Δ32–43); region 2, Δ69–84; region 3, Δ147–164; region 4, Δ202–206; region 5, Δ260–277; region 6, Δ295–301.

Fig. 2B. Western immunoblot from wildtype (wt) Erg27p and internal deletion strains. Erg27p was detected using HA-Probe (Y11) HRP antibody (1:500). Lcb1p, involved in sphingolipid biosynthesis, was used as a loading control and detected with anti-Lcb1p (1:500),

Fig. 2 — Fig. 2A. 3-ketoreductase sequence alignment with Erg27p internal deletions indicated as boxed areas. Homology plot of from Saccharomyces cerevisiae (top), Candida glabrata, Kluyvermyces lactis, Candida albicans, Mus musculus, Homo sapiens (bottom). Regions selected for internal deletions are outlined in red. Region 1 deleted amino acids 32–43 (Δ32–43); region 2, Δ69–84; region 3, Δ147–164; region 4, Δ202–206; region 5, Δ260–277; region 6, Δ295–301.

Fig. 2B. Western immunoblot from wildtype (wt) Erg27p and internal deletion strains. Erg27p was detected using HA-Probe (Y11) HRP antibody (1:500). Lcb1p, involved in sphingolipid biosynthesis, was used as a loading control and detected with anti-Lcb1p (1:500),