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Anti-KV1.1 (KCNA1) Antibody

Potassium voltage-gated channel subfamily A member 1

Cat #: APC-009
Alternative Name Potassium voltage-gated channel subfamily A member 1
Lyophilized Powder yes
Type: Polyclonal
Host: Rabbit
Reactivity: h, m, r
  • GST fusion protein with the sequence HRETEGEEQAQLLHV SSPNLASDSDLSRRSSSTISKSEYMEIEEDMNNSIAHYRQANIRTGNCTTADQNCVNKSKLLTDV, corresponding to amino acid residues 416-495 of mouse KV1.1 (Accession P16388). Intracellular, C-terminus.
Accession (Uniprot) Number P16388
Gene ID 16485
Peptide confirmation Confirmed by DNA sequence and SDS-PAGE.
Homology Rat - 78/80 amino acid residues identical; human - 76/80 amino acid residues identical; Xenopus Laevis - 70/80 amino acid residues identical.
RRID AB_2040144.
Purity The serum was depleted of anti-GST antibodies by affinity chromatography on immobilized GST and then the IgG fraction was purified on immobilized antigen.
Form Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
Isotype Rabbit IgG.
Storage before reconstitution The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
Reconstitution 25 µl, 50 µl or 0.2 ml double distilled water (DDW), depending on the sample size.
Antibody concentration after reconstitution 0.75 mg/ml.
Storage after reconstitution The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
Standard quality control of each lot Western blot analysis.
Applications: ic, if, ih, ip, wb
May also work in: ifc*
Western blot
  • Western blot analysis of rat brain membranes:
    Western blot analysis of rat brain membranes:
    1. Anti-KV1.1 (KCNA1) Antibody (#APC-009), (1:200).
    2. Anti-KV1.1 (KCNA1) Antibody, preincubated with Kv1.1/KCNA1 Blocking Peptide (#BLP-PC009).
  • Rat brain synaptosomes (Fili, O. et al. (2001) J. Neurosci. 21, 1964.).
  • Rat brain sections.
    Mouse sciatic nerve (1:200) (Zhou, L. et al. (1998) J. Neurosci. 18, 7200.).
  • Human neuromas (1:100) (England, J.D. et al. (1998) Neurosci. Lett. 255, 37.).
  1. Baumann, A. et al. (1988) EMBO J. 7, 2457.
  2. Gutman, G.A. et al. (2005) Pharmacol. Rev. 57, 473.
  3. Adelman, J.P. et al. (1995) Neuron 15, 1449.
  4. Bogin, O. (2006) Modulator 21, 28.
Scientific background

KV1.1 is a mammalian voltage-dependent K+ channel, homologous to the Drosophila Shaker K+ channel. KV1.1 was the first mammalian KV channel to be cloned from mouse brain.1 Eight Shaker-related genes exist in mammals constituting the KV1, subfamily of the large KV channel family of genes.2

A functional KV1 channel is either a membrane spanning homotetramer or heterotetramer, which is composed of members of the same subfamily. In addition several auxiliary subunits and intracellular proteins might interact with the channel and affect its function. The structure of KV1.1 channel is similar to all KV channels and includes six membrane spanning helices creating a voltage sensor domain and a pore domain.2

The channel is expressed in neurons and cardiac and skeletal muscle tissue as well as in the retina and pancreas.2 The functional channel is considered low voltage activated and shows very little inactivation. Therefore, this channel activity influences the membrane potential and excitability of neurons and muscle. Mutations in the coding of KV1.1 gene were discovered in Episodic Ataxia patients.3

KV1.1 channels are sensitive to low doses of TEA (0.3 mM) and 4-AP (0.29 mM), the “classical” non-selective potassium channel blockers.

Several venomous toxins from snakes, scorpions and sea anemones are potent blockers (affecting the channels in the nanomolar range) of KV1.1 channels. Among these, the most potent and selective are α-Dendrotoxin (0.4-4 nM) and δ-Dendrotoxin (0.03-1.8 nM), Dendrotoxin-K (0.03 nM), Agitoxin-2 (0.044 nM) and Hongotoxin-1 (0.031 nM).4

Application key:

CBE- Cell-based ELISA, FC- Flow cytometry, ICC- Immunocytochemistry, IE- Indirect ELISA, IF- Immunofluorescence, IFC- Indirect flow cytometry, IHC- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

Species reactivity key:

H- Human, M- Mouse, R- Rat
Image & Title:

Anti-Kv1.1 (KCNA1) Antibody
Expression of KV1.1 in mouse optic nerve.Immunohistochemical staining of mouse optic nerve sections using Anti-KV1.1 (KCNA1) Antibody (#APC-009). KV1.1 staining (red) is detected in the juxtaparanode region of the Nodes of Ranvier.Adapted from Bagchi, B. et al. (2014) PLoS ONE 9, e87736. with permission of PLoS.

Last update: 08/01/2023

Anti-KV1.1 (KCNA1) Antibody (#APC-009) is a highly specific antibody directed against an epitope of the mouse protein. The antibody can be used in western blot, immunohistochemistry, immunocytochemistry, and immunoprecipitation applications. It has been designed to recognize KV1.1 from human, rat, and mouse samples.

For research purposes only, not for human use



Western blot citations
  1. Human lung carcinoma cell line A549 isolated nuclei.
    Jang, S.H. et al. (2015) J. Biol. Chem. 290, 12547.
Immunoprecipitation citations
  1. Rat brain synaptosomes.
    Fili, O., et al. (2001) J. Neurosci. 21, 1964.
Immunohistochemistry citations
  1. Mouse optic nerve sections.
    Bagchi, B. et al. (2014) PLoS ONE 9, e87736.
  2. Mouse sciatic nerve (1:200).
    Chen, P. et al. (2014) FASEB J. 28, 1145.
  3. Mouse triangularis sterni muscle sections (1:200).
    Yao, D. et al. (2014) J. Neurosci. 34, 880.
  4. Zebrafish embryonic hindbrain (1:200).
    Brewster, D.L. and Ali, D.W. (2013) Neurosci. Lett. 539, 54.
  5. Mouse sciatic nerve (1:200).
    Zhou, L. et al. (1998) J. Neurosci. 18, 7200.
Immunocytochemistry citations
  1. Human Neuromas (1:100).
    England, J.D. et al. (1998) Neurosci. Lett. 255, 37.
More product citations
  1. Ovsepian, S.V. et al. (2013) J. Physiol. 591, 1771.
  2. Glaudemans, B. et al. (2009) J. Clin. Invest., 119, 936.
  3. Hsiao, C.F. et al. (2009) J. Neurophysiol. 101, 1407.
  4. Beraneck, M. et al. (2007) J. Neurosci. 27, 4283.
  5. Xuan, X. et al. (2007) J. Neurophysiol. 98, 2683.
  6. Knipper, M. et al. (2006) J. Physiol. 576, 73.
  7. Leao, R.N. et al. (2006) J. Physiol. 571, 563.
  8. Sinha, K. et al. (2006) J. Neurophysiol. 95, 1683.
  9. Devaux, J.J. and Scherer, S.S. (2005) J. Neurosci. 25, 1470.
  10. Kline, D.D. et al. (2005) J. Neurosci. 25, 3389.
  11. Wang, J. et al. (2005) Am. J. Physiol. Lung Mol. Cell Physiol. 288, L1049.
  12. Fukui, I. and Ohmori, H. (2004) J. Neuroscience 24, 7514.
  13. Karimi-Abdolrezaee, et al. (2004) Eur. J. Neurosci. 19, 577.
  14. Reid, M.A. et al. (2004) J. Neuroscience 24, 733.
  15. Dodson, P.D. et al. (2003) J. Physiol. 550.1 27.
  16. Grunnet, M. et al. (2003) Biophys. J. 85, 1525.
  17. Koni, P.A. et al. (2003) J. Biol. Chem. 278, 39443.
  18. Popratiloff, A. et al. (2003) J. Comparative Neurology 461, 466.
  19. Rios, J.C. et al. (2003) J. Neurosci. 23, 7001.
  20. Adamson, C.L. et al (2002) J. Neurosci. 22, 1385.
  21. Altevogt, B.M. et al (2002) J. Neurosci. 22, 6458.
  22. Arroyo, E.J. et al. (2002) J. Neurosci. 22, 1726.
  23. Chittajallu, R. et. al. (2002) PNAS 99, 2350.
  24. Dodson, P.D., et al (2002) J. Neurosci. 22, 6953.
  25. Felix, R. et al. (2002) Zygote 10, 183.
  26. Ji, J. et al. (2002) J. Biol. Chem. 277, 20195.
  27. McCormack, K. et al. (2002) J. Biol. Bhem. 277, 13219.
  28. Chung, Y.H. et al. (2000) Brain Res.875, 164.
  29. Keren-Raifman, T. et al. (2000) Biochem Biophys. Res. Commun. 274, 852.
  30. Nashmi, R. et al. (2000) Eur. J. Neurosci. 12, 491.
  31. Ouadid-Ahidouch, H., et al. (2000) Biochem. Biophys. Res. Commun. 278, 272.
  32. Singer-Lahat, D. et al. (2000) Eur J. Physiol. 440, 627.
  33. Arroyo, E.J. et al. (1999) J. Neurocytol. 28, 333.
  34. Sobko, A. et al. (1998) J. Neurosci. 18, 10398.


Scientific Background

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