Anti-H-ERG/KCNH2 Antibody Picoband® Fluoro488 Conjugated

KCNH2, also known as HERG or KV11.1, encodes the pore-forming subunit of a rapidly activating-delayed rectifier potassium channel. It is mapped to 7q36.1. KCNH2 forms the major portion of one of the ion channel proteins (the 'rapid' delayed rectifier current (IKr) ) that conducts potassium (K+) ions out of the muscle cells of the heart (cardiac myocytes), and this current is critical in correctly timing the return to the resting state (repolarization) of the cell membrane during the cardiac action potential. What’s more, KCNH2 channels show gating properties consistent with many of the outwardly rectifying potassium channels, but they also have an inactivation mechanism that attenuates efflux during depolarization.

Potassium voltage-gated channel subfamily H member 2; Eag homolog; Ether-a-go-go-related gene potassium channel 1; ERG-1; Eag-related protein 1; Ether-a-go-go-related protein 1; H-ERG; hERG-1; Herg1; Voltage-gated potassium channel subunit Kv11.1; KCNH2; ERG; ERG1; HERG

Cancer, Cancer Susceptibility, Epigenetics and Nuclear Signaling, Oncoproteins, Oncoproteins/Suppressors, Proto-Oncogenes, Signal Transduction, Transcription, Transcription Factors

Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) . Isoform A-USO: Has no channel activity by itself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation. Isoform B-USO: Has no channel activity by itself, but modulates channel characteristics by forming heterotetramers with other isoforms which are retained intracellularly and undergo ubiquitin-dependent degradation.

1. Gianulis, E. C., Trudeau, M. C. Rescue of aberrant gating by a genetically encoded PAS (Per-Arnt-Sim) domain in several long QT syndrome mutant human ether-a-go-go-related gene potassium channels. J. Biol. Chem. 286: 22160-22169, 2011. 2. Hedley PL; Jorgensen P; Schlamowitz S; Wangari, Romilda et al. (2009) . The genetic basis of long QT and short QT syndromes: a mutation update. Human Mutation 30 (11) : 1486–511. 3. Thomas, P. J., Qu, B.-H., Pedersen, P. L. Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20: 456-459, 1995.