Alomone Labs is pleased to offer the L-Type CaV Channel Blocker Explorer Kit (#EK-103). The Explorer Kit contains many classical L-type channel blockers, ideal for screening purposes.
Voltage-gated Ca2+ channels (CaV), enable the passage of Ca2+ ions in a voltage dependent manner. These heteromeric entities are formed in part by the pore-forming α1 subunit which determines the biophysical and pharmacological properties of the channel1.
L-type Ca2+ channels make up one of three voltage-gated Ca2+ channel families. Four different α1 isoforms (CaV1.1 to CaV1.4) belong to the L-type subfamily. Structurally, each α1 subunit has four homologous domains (I-IV) and each domain has a six transmembrane section. Like many other voltage-gated channels, L-type Ca2+ channels have auxiliary subunits which are responsible for modulating the surface expression and properties of the channels2-5.
CaV1.1 is mostly expressed in the skeletal muscle, while CaV1.4 is mainly detected in the retina. The expression of both CaV1.2 and CaV1.3 is more extensive and includes neurons, heart, smooth muscle, inner ear, retina and pancreas6. L-type Ca2+ channels are involved in and modulate a variety of physiological functions such as muscle contraction, hormone secretion, neuronal excitability and gene expression5.
All CaV1 channels are influenced by dihydropyridines (DHP) and are also referred to as DHP receptor. Several described peptidyl toxins are specific L-type channels blockers, but so far no selective blocker for CaV1 isoforms have been described.
- Zucotti, A. et al. (2011) Trends Pharmacol. Sci. 32, 366.
- Bauer, C.S. et al. (2010) Curr. Opin. Neurobiol. 20, 563.
- Dai, S. et al. (2009) Physiol. Rev. 89, 411.
- Davies, M. et al. (2007) Trends Pharmacol. Sci. 28, 220.
- Arikkath, J. and Campbell, K.P. (2003) Curr. Opin. Neurobiol. 13, 298.
- Catterall, W.A. (2000) Annu. Rev. Cell. Dev. Biol. 16, 521.