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. 1998 Apr 1;111(4):555–563. doi: 10.1085/jgp.111.4.555

Figure 1.

Figure 1

Figure 1

The S5–S6 linker region of Kv1.2, Kv1.3, and Kv3.1 potassium channels. (A) The amino acid sequence alignment of rKv1.2, hKv1.3, and rKv3.1 shows the S5 and S6 transmembrane domains, the pore-forming region (P region) and indicates the peptides used for generating the blocking antibodies (underlined). Dashes represent same amino acids as rKv1.2. (B) Schematic model showing the proposed arrangement of the external vestibule of Kv1.2 (drawn after Aiyar et al., 1995). The peptide used for generating the blocking antibody is in bold and shaded. Only the flanking S5 and S6 domains and two of the four subunits of the channel are illustrated. (C and D) Characterization of Kv1.2-BA and Kv1-NA antibodies. Membrane preparations from HEK-293 cells, untransfected (lane 1), transfected with Kv1.2 (lanes 2 and 4), or transfected with Kv1.3 (lane 3) were subjected to 10% SDS-PAGE and were Western blotted with Kv1.2-BA antibody (C) or Kv1-NA antibody (D). Lane 4 was probed with Kv1.2-BA that had been preincubated with the peptide used to generate Kv1.2-BA (C), or probed with Kv1-NA that had been preincubated with the peptide used to generate Kv1-NA (D). Estimated molecular masses of Kv1.2 and Kv1.3 were 70–80 kD. Bands representing endogenous Kv1 proteins could be seen upon longer exposure. (E) Characterization of Kv3.1-BA antibody. Membrane preparations from HEK-293 cells, untransfected (lane 1), transfected with Kv3.1 (lanes 2 and 4), or transfected with Kv1.2 (lane 3) were subjected to SDS-PAGE and were Western blotted with Kv3.1-BA antibody. Lane 4 was probed with Kv3.1-BA that had been preincubated with the peptide used to generate Kv3.1-BA. Estimated molecular mass of Kv3.1 was 100 kD. Positions of prestained molecular mass markers in kilodaltons are indicated on the left.

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