Overview
- Peptide (C)DERELLRHPPVP(K), corresponding to amino acid residues 268-279 of rat KV1.5 (Accession P19024). 1st extracellular loop.
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).
Expression of KV1.5 channels in rat cerebellumImmunohistochemical 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).
- PASMCs transfected with KV1.5 (Lv, Y. et al. (2013) Am. J. Physiol. 305, L856.).
Cell surface detection of KV1.5 by indirect flow cytometry in live intact human THP-1 monocytic leukemia cells:___ Cells.
___ Cells + goat-anti-rabbit-FITC.
___ Cells + Anti-KV1.5 (KCNA5) (extracellular) Antibody (#APC-150), (5μg) + goat-anti-rabbit-FITC.- The blocking peptide is not suitable for this application.
- Swanson, R. et al. (1990) Neuron 4, 929.
- Gutman, G.A. et al. (2005) Pharmacol. Rev. 57, 473.
- McGahon, M.K. et al. (2007) Am. J. Physiol. Heart Circ. Physiol. 292, H1001.
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
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.
Applications
Citations
Powered by Bioz- Human smooth muscle cell lysate (1:1000).
Nishijima, Y. et al. (2017) Circ. Res. 120, 658.
- Human adipose tissue sections.
Nishijima, Y. et al. (2017) Circ. Res. 120, 658.
- Mouse isolated cardiomyocytes.
Kilfoil, P.J. et al. (2019) J. Mol. Cell. Cardiol. 137, 93. - Human smooth muscle cells (1:200).
Nishijima, Y. et al. (2017) Circ. Res. 120, 658. - CHO transfected cells.
Crump, S.M. et al. (2016) FASEB J. 30, 360. - HEK 293 transfected cells.
Jimenez-Perez, L. et al. (2016) J. Biol. Chem. pii: jbc.M115.678995. - PASMCs transfected with KV1.5.
Lv, Y. et al. (2013) Am. J. Physiol. 305, L856.
