Overview
- Peptide DRLPKSDSEDGPRALNQLSC, corresponding to amino acid residues 493-511 of rat NaV1.5 (Accession P15389). Intracellular loop between domains I and II.
- Human-NaV1.5 transfected HEK-293 cells, rat heart membrane protein (1:200-1:500).
Western blot analysis of human-NaV1.5 transfected HEK-293 cell lysate (lanes 1 and 3) and rat heart membrane protein (lanes 2 and 4):1,2. Guinea pig Anti-NaV1.5 (SCN5A) Antibody (#ASC-005-GP), (1:200).
3,4. Guinea pig Anti-NaV1.5 (SCN5A) Antibody, preincubated with Nav1.5/SCN5A (493-511) Blocking Peptide (#BLP-SC005).- Following a broad screen of secondary antibodies, the following was used for this application: #106-035-006 (Jackson ImmunoResearch).
- Rat heart sections.
- Human heart sections (1:200) (Cheng, J. et al. (2017) Sci. Rep. 7, 42953.).
Voltage-gated Na+ channels (NaV) are responsible for myocardial conduction and maintenance of the cardiac rhythm and are essential for the generation of action potentials and cell excitability1.
Dysfunction or disregulation of cardiac sodium channels can cause several disorders, including cardiac arrhythmias.
The majority of Na+ channels in the mammalian heart are Tetrodotoxin (TTX)-insensitive NaV1.52.
The putative structure of NaV1.5 consists of four homologous domain (I-IV), each containing six transmembrane segments (S1-S6). Mutations in the C-terminus of NaV1.5 were described in connection to Long QT syndrome and Brugada syndrome1,2. Recent data have demonstrated selective expression of NaV1.5 in the mouse central nervous system and implicated a role for NaV1.5 in the physiology of the central nervous system1.
Multiplex staining of NaV1.5 and Vinculin in human heart.Immunohistochemical staining of human ventricle heart sections using Guinea pig Anti-NaV1.5 (SCN5A) Antibody (#ASC-005-GP) and mouse anti-vinculin antibody. NaV1.5 staining (green) is detected in intercalated disks and co-localizes with vinculin.Adapted from Cheng, J. et al. (2017) Sci. Rep. 7, 42953. with permission of SPRINGER NATURE.
