Journal: The Journal of Cell Biology
Article Title: Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments
doi: 10.1083/jcb.200109026
Figure Lengend Snippet: Targeting of β IV spectrin, Na v 1.6, NrCAM, and neurofascin to Purkinje neuron initial segments is disrupted in ankyrin-G cerebellum- specific knockout mice. Cerebellar sections from wild-type (A, D, G, J, and M) or cerebellar ankyrin-G knockout mice (B, C, E, F, H, I, K, L, N, and O) were double labeled with antibodies against calbindin (red in A–F; green in G–L) and either ankyrin-G (green in A–C), βIV spectrin (green in D–F), Na v 1.6 (red in G–I), NrCAM (red in J–L), or neurofascin (M–O). All images except M–O are composites. Bars: (A, B, and E) 5 μm; (C, D, F, G, I, and J–O) 10 μm; and (H) 25 μm.
Article Snippet: Antibodies used include a mouse monoclonal antibody against the ankyrin-G spectrin–binding domain ( ); affinity-purified rabbit polyclonal antibodies against neurofascin , NrCAM ( ) and the peptide CIANHTGVDIHRNGDFQKNG corresponding to residues 1042–1061 of mouse or rat Na v 1.6 (Alomone Labs); a goat polyclonal antibody against calbindin (Santa Cruz Biotech), and a chicken polyclonal antibody against the βIV spectrin unique domain that has been adsorbed against brain lysate from a βIV spectrin knockout mouse (gift of Dr. M. Komada, Tokyo Institute of Technology, Tokyo, Japan).
Techniques: Knock-Out, Labeling