Data supplements
JEB032151 Supplementary Material
Files in this Data Supplement:
- Supplemental Table S1 -
- Supplemental Figure S1
-
Fig. S1. The amplification of alternative oxidase (AOX) transcripts from three animal species (Pacific oyster, Crassostrea gigas; Eastern oyster, Crassostrea virginica and the freshwater sponge, Ephydatia muelleri) using RT-PCR and degenerate animal AOX primers. The positive control from the RT-PCR kit is 323.bp in size whereas AOX transcripts are ∼400.bp.
- Supplemental Figure S2
-
Fig. S2. A multiple sequence alignment of full-length and partial animal alternative oxidase (AOX) proteins from different phyla. The arrows denote the conserved glutamate (E) and histidine (H) residues required for iron binding. The bracket highlights a region of the C-terminus that contains a sequence unique to animal AOX proteins. The black bar represents the epitope region recognized by the AOX antibody (AOA).
JEB032151 Supplementary Material
Files in this Data Supplement:
- Supplemental Table S1 -
- Supplemental Figure S1
-
Fig. S1. The amplification of alternative oxidase (AOX) transcripts from three animal species (Pacific oyster, Crassostrea gigas; Eastern oyster, Crassostrea virginica and the freshwater sponge, Ephydatia muelleri) using RT-PCR and degenerate animal AOX primers. The positive control from the RT-PCR kit is 323.bp in size whereas AOX transcripts are ∼400.bp.
- Supplemental Figure S2
-
Fig. S2. A multiple sequence alignment of full-length and partial animal alternative oxidase (AOX) proteins from different phyla. The arrows denote the conserved glutamate (E) and histidine (H) residues required for iron binding. The bracket highlights a region of the C-terminus that contains a sequence unique to animal AOX proteins. The black bar represents the epitope region recognized by the AOX antibody (AOA).