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Anti-KV1.5 (KCNA5) (extracellular) Antibody

Potassium voltage-gated channel subfamily A member 5
Cat #: APC-150
Alternative Name Potassium voltage-gated channel subfamily A member 5
Lyophilized Powder yes
Type: Polyclonal
Host: Rabbit
Reactivity: h, r
May also work in: m*
Immunogen
  • Peptide (C)DERELLRHPPVP(K), corresponding to amino acid residues 268-279 of rat KV1.5 (Accession P19024). 1st extracellular loop.
Accession (Uniprot) Number P19024
Gene ID 25470
Peptide confirmation Confirmed by amino acid analysis and mass spectrometry.
Homology Rat - 12/13 amino acid residues identical; human - 11/13 amino acid residues identical; mouse - 9/13 amino acid residues identical.
RRID AB_10918640.
Purity Affinity 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 0.8 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, ifc, ih, wb
May also work in: ip*, lci*
Western blot
  • Western blot analysis of rat brain membranes:
    Western blot analysis of rat brain membranes:
    1. Anti-KV1.5 (KCNA5) (extracellular) Antibody (#APC-150), (1:200).
    2. Anti-KV1.5 (KCNA5) (extracellular) Antibody, preincubated with Kv1.5/KCNA5 (extracellular) Blocking Peptide (#BLP-PC150).
Immunohistochemistry
  • Expression of KV1.5 channels in rat cerebellum
    Expression of KV1.5 channels in rat cerebellum
    Immunohistochemical staining of rat cerebellum with Anti-KV1.5 (KCNA5) (extracellular) Antibody (#APC-150), (1:200). A. KV1.5 (green) appears in both the soma of Purkinje cells (horizontal arrows) and in Purkinje dendrites (vertical arrows). B. Neurons expressing gamma amino butyric acid (GABA) were labeled with mouse anti-parvalbumin antibody (red). C. Merge of the two images demonstrates partial colocalization (white arrows).
Immunocytochemistry
  • PASMCs transfected with KV1.5 (Lv, Y. et al. (2013) Am. J. Physiol. 305, L856.).
Indirect flow cytometry
  • Cell surface detection of KV1.5 in live intact THP-1 (human acute monocytic leukemia cells) cell line:
    Cell surface detection of KV1.5 in live intact THP-1 (human acute monocytic leukemia cells) cell line:
    ___ Cells + Goat-anti-rabbit-Cy5.
    ___ Cells + Anti-KV1.5 (KCNA5) (extracellular) Antibody (#APC-150), (1:20) + goat-anti-rabbit-Cy5.
  • The blocking peptide is not suitable for this application.
References
  1. Swanson, R. et al. (1990) Neuron 4, 929.
  2. Gutman, G.A. et al. (2005) Pharmacol. Rev. 57, 473.
  3. McGahon, M.K. et al. (2007) Am. J. Physiol. Heart Circ. Physiol. 292, H1001.
Scientific background

KV1.5 is a mammalian voltage dependent K+ channel, homologous to the Drosophila Shaker K+ channel. KV1.5 was first cloned from the rat 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 KV1.5 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 cardiac and smooth muscle tissue (colon, aorta, stomach and pulmonary artery) as well as in neurons and kidney.2 A loss-of-function mutation in the gene encoding the channel was found in atrial fibrillation patients, stressing its role as a cardiac action potential regulator.3

The functional channel is considered transient (A-type) channel and shows prominent inactivation. Therefore, this channel activity influences the membrane potential and excitability of neurons and muscle.

KV1.5 channels are sensitive to high doses of TEA (330 mM) and low doses of 4-AP (0.27 mM), the “classical” non-selective potassium channel blockers.2

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
Last update: 16/08/2020

Anti-KV1.5 (KCNA5) (extracellular) Antibody (#APC-150) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot, immunohistochemistry, immunocytochemistry, and indirect flow cytometry. This antibody recognizes an extracellular epitope and thus is ideally suited to detect KV1.5 in living cells. It has been designed to recognize KV1.5 from human, mouse, and rat samples.

For research purposes only, not for human use

Applications

Specifications

Scientific Background

Citations

Citations
Western blot citations
  1. Human smooth muscle cell lysate (1:1000).
    Nishijima, Y. et al. (2017) Circ. Res. 120, 658.
Immunohistochemistry citations
  1. Human adipose tissue sections.
    Nishijima, Y. et al. (2017) Circ. Res. 120, 658.
Immunocytochemistry citations
  1. Mouse isolated cardiomyocytes.
    Kilfoil, P.J. et al. (2019) J. Mol. Cell. Cardiol. 137, 93.
  2. Human smooth muscle cells (1:200).
    Nishijima, Y. et al. (2017) Circ. Res. 120, 658.
  3. CHO transfected cells.
    Crump, S.M. et al. (2016) FASEB J. 30, 360.
  4. HEK 293 transfected cells.
    Jimenez-Perez, L. et al. (2016) J. Biol. Chem. pii: jbc.M115.678995.
  5. PASMCs transfected with KV1.5.
    Lv, Y. et al. (2013) Am. J. Physiol. 305, L856.
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