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- Peptide (C)EFTSIGRSR IMGLSE, corresponding to amino acid residues 446-460 of rat NaV1.7 (Accession O08562). Intracellular loop between domains I and II.
- Expression of NaV1.7 in rat DRGImmunohistochemical staining of rat dorsal root ganglion (DRG) using Anti-NaV1.7 (SCN9A)-ATTO-633 Antibody (#ASC-008-FR). A. NaV1.7 staining (purple) appears in DRG neurons. B. Nuclear staining using DAPI as the counterstain. C. Merge images of A and B.
- 1. Wu, L. et al. (2002) NeuroReport 13, 2547.
- 2. Fang, X. et al. (2002) J. Neurosci. 22, 7425.
- 3. Fjell, J. et al. (2000) NeuroReport 11, 199.
- 4. Baker, M.D. and Wood, J.N. (2001) Trends Pharmacol. Sci. 22, 27.
- 5. Lai, J. et al. (2003) Curr. Opin. Neurobiol. 13, 291.
- 6. Isom, L.L. (2001) Neuroscientist 7, 42.
- 7. Catterall, W.A. et al. (2003) Pharmacol. Rev. 55, 575.
- 8. Catterall, W.A. et al. (2005) Pharmacol. Rev. 57, 397.
- 9. Yang, Y. et al. (2004) J. Med. Genet. 41, 171.
- 10. Cummins, T.R. et al. (2004) J. Neurosci. 24, 8232.
- 11. Dray, A. (2008) Br. J. Anaesth. 101, 48.
Voltage-gated sodium channels (NaV) are essential for the generation of action potentials and for cell excitability1. NaV channels are activated in response to depolarization and selectively allow the flow of Na+ ions. To date, nine NaV α subunits have been cloned and named NaV1.1-NaV1.94-5. The NaV channels are classified into two groups according to their sensitivity to tetrodotoxin (TTX): TTX-sensitive (NaV1.1, NaV1.2, NaV1.3, NaV1.4, NaV1.6 and NaV1.7) and TTX-resistant (NaV1.5, NaV1.8 and NaV1.9)2-3.
Mammalian sodium channels are heterotrimers composed of a central, pore-forming α subunit and two auxiliary β subunits. The expression of the α subunit isoform is developmentally regulated and tissue specific. Na+ channels in the adult central nervous system and heart contain β1 through β4 subunits, whereas Na+ channels in adult skeletal muscle have only the β1 subunit6,8.
NaV1.7 is predominantly expressed in dorsal root ganglions (DRG) of the peripheral nervous system. Dominant gain of function mutations in the NaV1.7 gene are associated with erythermalgia (a rare autosomal disease characterized by sporadic burning pain accompanied by redness and heat in the extremities).9-11 Loss of function mutations in NaV1.7 channels leads to complete ablation of pain perception in humans.11 These recent findings highlight the role of this NaV isoform and the subset of DRG neurons that express this channel in physiological pain sensation.
Species reactivity key:
Anti-NaV1.7 (SCN9A) Antibody (#ASC-008) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunohistochemistry, and immunocytochemistry applications. It has been designed to recognize NaV1.7 from rat, human, and mouse samples.
Anti-NaV1.7 (SCN9A)-ATTO-633 Antibody (#ASC-008-FR) is directly labeled with an ATTO-633 fluorescent dye. ATTO dyes are characterized by strong absorption (high extinction coefficient), high fluorescence quantum yield, and high photo-stability. ATTO 633 has a maximum absorption at 629 nm and a maximum fluorescence at 657 nm. The fluorescence is excited most efficiently in the range 610 to 645 nm. This label is analogous to the well-known dyes Alexa 647, Alexa 633 and Cy5. Anti-NaV1.7 (SCN9A)-ATTO-633 Antibody is especially suited for experiments requiring simultaneous labeling of different markers.
- Guinea pig Anti-NaV1.7 (SCN9A) Antibody (#AGP-057) is raised in guinea pig and can be used in immuno-colocalization studies in conjunction with any of our antibodies raised in rabbit. This antibody has been raised against the same epitope as #ASC-008.
- Blockers/Antagonists: peptides/peptide toxinsBlockers/Antagonists: small molecules