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Anti-KCNH2 (HERG) Antibody

KV11.1, Potassium voltage-gated channel subfamily H member 2, Ether-a-go-go-related channel 1
Cat #: APC-062
Alternative Name KV11.1, Potassium voltage-gated channel subfamily H member 2, Ether-a-go-go-related channel 1
Lyophilized Powder yes
Type: Polyclonal
Host: Rabbit
Reactivity: h, m, r
Immunogen
  • GST fusion protein with the sequence DSLSQVSQFMACEELPPGAPELPQEGPTRRLSLPGQLGALTSQPLHRHGSDPGS, corresponding to amino acid residues 1106-1159 of human KV11.1 (HERG) (Accession Q12809). Intracellular, C-terminus.
Accession (Uniprot) Number Q12809
Gene ID 3757
Peptide confirmation Confirmed by DNA sequence and SDS-PAGE.
Homology Rabbit - identical; dog - 51/54 amino acid residues identical; mouse, rat - 50/54 amino acid residues identical.
RRID AB_2039908.
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.
Specificity The antibody recognizes the HERG1b splice variant but not splice variants HERG1-3 and HERG-4
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 0.6 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 KV11.1 (HERG)-expressing HEK-293 cells:
    Western blot analysis of KV11.1 (HERG)-expressing HEK-293 cells:
    1. Anti-KCNH2 (HERG) Antibody (#APC-062), (1:400).
    2. Anti-KCNH2 (HERG) Antibody, preincubated with KCNH2/HERG Blocking Peptide (#BLP-PC062).
  • Neonatal rat ventricular myocytes (NRVMs) (Dennis, A.T. et al. (2011) J. Biol. Chem. 286, 34413.).
Immunoprecipitation
  • Immunoprecipitation of KV11.1-expressing HEK-293 cells:
    Immunoprecipitation of KV11.1-expressing HEK-293 cells:
    1. Cell lysate.
    2. Cell lysate + protein A beads + Anti-KCNH2 (HERG) Antibody (#APC-062).
    3. Cell lysate + protein A beads + Anti-KCNH2 (erg1) Antibody (#APC-016).
    4. Cell lysate + protein A beads + Anti-KCNH2 (HERG) (extracellular) Antibody (#APC-109).
    5. Cell lysate + protein A beads + pre-immune rabbit serum.

    Red arrow indicates KV11.1 while the black arrow shows the IgG heavy chain.
    Immunoblot was performed with the Anti-KCNH2 (HERG) Antibody.
Immunohistochemistry
  • Mouse frozen heart sections (1:300) (Teng, G.Q. et al. (2008) Circ. Res. 103, 1483.).
Immunocytochemistry
  • Expression of KV11.1 (HERG) in HEK-293 transfected cells
    Expression of KV11.1 (HERG) in HEK-293 transfected cells
    Immunocytochemical staining of fixed and permeabilized KV11.1 transfected HEK-293 cells. Cells were stained with Anti-KCNH2 (HERG) Antibody (#APC-062), followed by goat anti-rabbit-AlexaFluor-555 secondary antibody (Red). Almost all transfected cells are stained positive for the KV11.1. Arrows indicate cells that do not express the channel.
References
  1. Curran, M.E. et al. (1995) Cell 80, 795
  2. Sanguinetti, M.C. et al. (1995) Cell 81, 299.
  3. Pardo, L.A. et al. (2004) Physiology 19, 285.
  4. Gurrola, G.B. et al. (1999) FASEB. J. 13, 953.
  5. Korolkova, Y.V. et al. (2001) J. Biol. Chem. 276, 9868.
  6. Zhou, Z. et al. (1998) Biophys. J. 74, 230.
Scientific background

The KV11.1 (HERG) channel is a member of the ether-a-go-go (EAG) subfamily of voltage-dependent K+ channels that includes the related proteins KV11.2 and KV11.3 (erg2 and erg3). KV11.1 possesses the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains and intracellular N- and C-termini.

The KV11.1 current is characterized by strong inward rectification with slow activation and very rapid inactivation kinetics. The channel is expressed in the brain and heart (where it underlies the IKr current) and has a central role in mediating repolarization of action potentials.1,2

Mutations in the KV11.1 channel cause inherited long QT syndrome (LQTS) or abnormalities in the repolarization of the heart that are associated with life-threatening arrhythmias and sudden death. All the identified KV11.1 mutations produce loss of function of the channel via several cellular mechanisms ranging from alterations of gating properties, alterations of channel permeability/selectivity and alterations in intracellular channel trafficking that decreases the number of channels that reach the cell membrane.1,2 

Recently, drug-induced forms of LQTS have been reported for a wide range of non-cardiac drugs including antihistamines, psychoactive agents and antimicrobials. All these drugs potently block the KV11.1 channel as an unintended side effect, prompting regulatory drug agencies to issue recommendations for the testing of new drugs for their potential KV11.1 blocking effect.

In addition, KV11.1 expression was found to be upregulated in several tumor cell lines of different histogenesis, suggesting that it confers the cells some advantage in cell proliferation. Indeed, in several studies it has been shown that inhibition of the KV11.1 current leads to a decrease in tumor cell proliferation.3

Several toxins from scorpion venoms are potent blockers (affecting the channels in the nanomolar range) of KV11.1 channels. Among these the most potent and selective are Ergtoxin-1 (16 nM)4 and BeKM-1 (3 nM).5 In addition, the methanesulfonanilide class III antiarrhythmic agent E-4031 also blocks KV11.1 channel in the nanomolar range (7.7 nM).6

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: 10/09/2020

Alomone Labs is pleased to offer a highly specific antibody directed against an intracellular epitope of the human KV11.1 channel. Anti-KCNH2 (HERG) Antibody (#APC-062) can be used in western blot, immunoprecipitation, immunohistochemical and immunocytochemical applications. It has been designed to recognize KV11.1 from human, rat, and mouse samples.

For research purposes only, not for human use

Applications

Specifications

Scientific Background

Citations

Citations
Western blot citations
  1. HeLa-transfected cells.
    Hantouche, C. et al. (2017) J. Biol. Chem. 292, 2287.
  2. HEK 293 cells transfected with hERG.
    Varkevisser, R. et al. (2013) Br. J. Pharmacol. 169, 1322.
  3. Neonatal rat ventricular myocytes (NRVMs).
    Dennis, A.T. et al. (2011) J. Biol. Chem. 286, 34413.
Immunoprecipitation citations
  1. HeLa-transfected cells.
    Hantouche, C. et al. (2017) J. Biol. Chem. 292, 2287.
  2. HeLa cells transfected with hERG.
    Apaja, P.M. et al. (2013) Mol. Biol. Cell 24, 3787.
Immunohistochemistry citations
  1. Mouse frozen heart sections (1:300).
    Teng, G.Q. et al. (2008) Circ. Res. 103, 1483.
Immunocytochemistry citations
  1. HEK 293 cells transfected with hERG.
    Varkevisser, R. et al. (2013) Br. J. Pharmacol. 169, 1322.
More product citations
  1. David, J.P. et al. (2013) Traffic 14, 399.
  2. Organ-Darling, L.E. et al. (2013) Am. J. Physiol. 304, H589.
  3. Aidery, P. et al. (2012) Biochem. Biophys. Res. Com. 418, 830.
  4. Dennis, A.T. et al. (2012) Mol. Pharmacol. 81, 198.
  5. Albesa, M. et al. (2011) J. Mol. Cell. Cardiol. 51, 90.
  6. Nalos, L. et al. (2011) Eur. J. Pharmacol. 652, 96.
  7. Ganapathi, S.B. et al. (2010) Am. J. Physiol. Cell Physiol. 299, C74.
  8. Hayashi, K. et al. (2010) Heart Rhythm. 7, 973.
  9. Ren, X.Q. et al. (2010) Am. J. Physiol. Heart Circ. Physiol. 299, H1525.
  10. Nanduri, J. et al. (2009) Biochem. Biophys. Res. Com. 388, 212.
  11. Huo, J. et al. (2008) Pflugers Arch 456, 917.
  12. Nanduri, J. et al. (2008) Biochem. Biophys. Res. Com. 373, 309.
  13. Roy, J. et al. (2008) Oncol. Rep. 19, 1511.
  14. Nakajima, T. et al. (2007) J. Biol. Chem. 282, 5506.
  15. Sun, H. et al. (2006) J. Biol. Chem. 281, 5877.
  16. Chapman, H. et al. (2005) J. Cell Sci. 118, 5325.
  17. Rossenbacker, T. et al. (2005) Circulation 111, 961.
  18. Ficker, E. et al. (2003) Circ. Res. 92, 87.
  19. Shoeb, F. et al. (2003) J. Biol. Chem. 278, 2503.
  20. Zicha, S. et al. (2003) Am. J. Physiol. Heart Circ. Physiol. 285, H1641.
  21. Finley, M. R. et al. (2002) Am. J. Physiol. Heart Circ. Physiol. 283, 126.
  22. Paulussen, A. et al. (2002) J. Biol. Chem. 277, 48610.
  23. Pillozzi, S. et al. (2002) Leukemia 16, 1791.
  24. Smith, G.A. et al. (2002) J. Biol. Chem. 277, 18528.
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