Overview
- Peptide (CY)HMLPGGGAHGSTRDQSI, corresponding to amino acid residues 841-857 of rat KV2.1 (Accession P15387). Intracellular, C-terminus.
Western blot analysis of rat brain membranes:1. Anti-KV2.1 Antibody (#APC-012), (1:500).
2. Anti-KV2.1 Antibody, preincubated with KV2.1 Blocking Peptide (BLP-PC012).
- Xenopus oocyte membranes (MacDonald, P.E. et al. (2002) Mol. Endocrinol. 16, 2452.).
Expression of KV2.1 channel in rat pancreasImmunohistochemical staining of rat paraffin embedded pancreas sections using Anti-KV2.1 Antibody (#APC-012), (1:50), followed by goat anti-rabbit-AlexaFluor-555 secondary antibody. Endocrine (Islets of Langerhans) and exocrine areas of pancreas section are shown. Strong and highly specific KV2.1 staining is evident only in endocrine cells (red). Hoechst 33342 is used as the counterstain (blue).- Mouse pancreas sections (10 μg/ml) (MacDonald, P.E. et al. (2002) J. Biol. Chem. 277, 44938.).
Human brain sections (1:500) (Mezey, E. et al. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 1364.).
- Mouse DRGs (Bocksteins, E. et al. (2009) Am. J. Physiol. 296, C1271.).
- Albrecht, B. et al. (1993) Receptors Channels 1, 99.
- Murakoshi, H. and Trimmer, J.S. (1999) J. Neurosci. 19, 1728.
- Archer, S.L. et al. (1998) J. Clin. Invest. 101, 2319.
- Escoubas, P. et al. (2002) Mol. Pharmacol. 62, 48.
KV2.1 is a member of the voltage-gated K+ channel superfamily. Together with the closely related KV2.2 protein they form the KV2 subfamily also known as Shab.1
As with all KV channels, KV2.1 possesses the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains with intracellular N and C termini. The functional KV channel is a tetramer that can either be a homotetramer or a heteromer of KV2.1 and KV2.2 subunits.
Both KV2.1 and KV2.2 channels are known as delayed rectifiers that is, channels that are activated by changes in membrane potential (depolarization) but inactivate very slowly. The current they form is known as IK or IDR. Accessory subunits such as KChaP and the electrically silent a subunits KV8 and KV9 can modulate biochemical and biophysical properties of KV2.1.2
KV2.1 is widely expressed throughout the body including brain, lung, pancreas, skeletal muscle and pulmonary artery.2
The main function of KV2.1 is to maintain membrane potential and to modulate the electrical excitability in neurons and muscle. In rat pulmonary artery it probably mediates hypoxic pulmonary vasoconstriction together with the KV9.3 subunit.3
Several toxins from spider venoms are potent blockers (affecting the channels in the nanomolar range) of KV2.1 channels. Among these the most potent and selective are Stromatoxin-1 (#STS-350), (12.7 nM)4 and Hanatoxin (42 nM).4
Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of the rat KV2.1 channel. Anti-KV2.1 Antibody (#APC-012) can be used in western blot, immunoprecipitation, immunocytochemistry, and immunohistochemistry applications. It has been designed to recognize KV2.1 from rat, human, and mouse samples.
Applications
Citations
Powered by Bioz- Human myometrium tissue lysate.
Novakovic, R. et al. (2015) Mol. Hum. Reprod. 21, 545. - Rat uterine tissue lysate.
Novakovic, R. et al. (2013) J. Physiol. Pharmacol. 64, 795. - Rat lung lysate.
Lv, Y. et al. (2013) Am. J. Physiol. 305, L856. - Mouse heart lysate.
Huang, H. et al. (2013) J. Mol. Cell. Cardiol. 59, 151.
- Xenopus oocyte membranes.
MacDonald, P.E. et al. (2002) Mol. Endocrinol. 16, 2452.
- Rat lumbar spinal cord sections.
Wolff, M. et al. (2016) Neurosci. Res. 109, 16. - Mouse brain sections.
Peltola, M.A. et al. (2016) Schizophr. Bull. 42, 191. - Human myometrium sections (1:50).
Novakovic, R. et al. (2015) Mol. Hum. Reprod. 21, 545. - Mouse brain sections (1:250).
Baver, S.B. et al. (2014) J. Neurosci. 34, 5486. - Human artery tissues (1:50).
Gojkovic-Bukarica, L. et al. (2011) Eur. J. Pharmacol. 654, 266. - Human brain sections (1:500).
Mezey, E. et al. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 1364. - Mouse pancreas sections (10 μg/ml).
MacDonald, P.E. et al. (2002) J. Biol. Chem. 277, 44938.
- Mouse DRGs.
Bocksteins, E. et al. (2009) Am. J. Physiol. 296, C1271.
- Mouse DRG neurons.
Regnier, G. et al. (2016) Physiol. Rep. 4, e12731. - Mouse ETV1 cells.
Bishop, H.I. et al. (2015) J. Neurosci. 35, 14922.
- Tiran, Z. et al. (2003) J. Biol. Chem. 278, 17509.
- MacDonald, P.E. et al. (2002) Diabetes 51, 443.
- Platoshyn, O. et al. (2001) Am. J. Physiol. 280, L801.
- Reeve, H.L. et al. (2001) J. Appl. Physiol. 90, 2249.
- Trepanier-Boulay, V. et al. (2001) Circ. Res. 89, 437.
- Betancourt, L. et al. (2000) J. Neurosci. Res. 61, 646.
- Yamashita, T. et al. (2000) Circulation 101, 2007.
