Antigen: fusion protein amino acids 1,019-1,293 (II-III loop) human Cav3.2 · Clone designation: S55-10 · Host: Mouse · Isotype: IgG1 · Application(s): WB, IHC, and ICC · Ion channels are integral membrane proteins that help establish and control the small voltage gradient across the plasma membrane of living cells by allowing the flow of ions down their electrochemical gradient.¹ They are present in the membranes that surround all biological cells and their main function is to regulate the flow of ions across this membrane. Whereas some ion channels permit the passage of ions based on charge, others conduct based on a ionic species, such as sodium or potassium. Furthermore, in some ion channels, the passage is governed by a gate which is controlled by chemical or electrical signals, temperature, or mechanical forces. There are a few main classifications of gated ion channels. There are voltage-gated ion channels, ligand-gated, other gating systems, and finally those that are classified differently, having more exotic characteristics. The first are voltage-gated ion channels which open and close in response to membrane potential. These are then seperated into sodium, calcium, potassium, proton, transient receptor, and cyclic nucleotide-gated channels, each of which is responsible for a unique role. Ligand-gated ion channels are also known as ionotropic receptors and they open in response to specific ligand molecules binding to the extracellular domain of the receptor protein. The other gated classifications include activation and inactivation by second messengers, inward-rectifier potassium channels, calcium-activated potassium channels, two-pore-domain potassium channels, light-gated channels, mechano-sensitive ion channels, and cyclic nucleotide-gated channels. Finally, the other classifications are based on less normal characteristics such as two-pore channels and transient receptor potential channels.² Cav3.2 is a protein which in humans is encoded by the CACNA1H gene. Studies suggest certain mutations in this gene lead to childhood absence epilepsy.^3,4 Studies also suggest that the up-regulations of Cav3.2 may participate in the progession of prostate cancer toward an androgen-independent stage.⁵

1 Hille, B. Ion Channels of Excitable Membranes. (2001).

2 What are ion channels?. (2004).

3 Chen, Y., Lu, J., Pan, H., et al. Associated between genetic variation of CACNA1H and childhood absence epilepsy. Ann Neurol 54(2) 239-243 (2003).

4 Khosravani, H., Altier, C., Simms, B., et al. Gating effects of mutations in the Cav3.2 T-type calcium channel associated with childhood absence epilepsy. J Biol Chem 279(11) 9681-9684 (2004).

5 Gackière, F., Bidaux, G., Delcourt, P., et al. Cav3.2 T-type calcium channels are involved in calcium-dependent secretion of neuroendocrine prostate cancer cells. J Biol Chem 283(15) 10162-10173 (2008).

Hille, B. Ion Channels of Excitable Membranes. (2001).

Gackière, F., Bidaux, G., Delcourt, P., et al. Cav3.2 T-type calcium channels are involved in calcium-dependent secretion of neuroendocrine prostate cancer cells. J Biol Chem 283(15) 10162-10173 (2008).

Khosravani, H., Altier, C., Simms, B., et al. Gating effects of mutations in the Cav3.2 T-type calcium channel associated with childhood absence epilepsy. J Biol Chem 279(11) 9681-9684 (2004).

Chen, Y., Lu, J., Pan, H., et al. Associated between genetic variation of CACNA1H and childhood absence epilepsy. Ann Neurol 54(2) 239-243 (2003).

What are ion channels?. (2004).

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