CaV1.2 | voltage-dependent, L type, alpha 1C subunit calcium channel

Calcium channels

L-Type (CaV1.1–CaV1.4), P/Q-Type (CaV2.1), N-Type (CaV2.2), R-Type (CaV2.3), T-Type (CaV3.1–CaV3.3)

Six transmembrane alpha helices (S1–S6), total of four homologous domains make up the tetrameric alpha subunit structure

One large alpha subunit forms a functional channel, accessory subunits ( α1, α2δ, β1-4, and γ) are crucial for robust expression, they functionally modulate the alpha subunit

CaV1.2: Background Information

CaV1.2 is a subunit of L-type voltage-dependent calcium channel. In the heart it forms a complex with the subunits β2 and α2δ1 in a 1:1:1 ratio. The alpha-1 consists of 24 transmembrane segments and is the pore forming element through which ions pass into the cell, whereas the β2 and α2δ1 subunits modulate the channel function. CaV1.2 is widely expressed in the smooth muscle, pancreatic cells, fibroblasts, and neurons. However, it is particularly important and well known for its expression in the heart where it mediates L-type currents, which causes calcium-induced calcium release from the ER Stores via ryanodine receptors. It depolarizes at -30 mV and helps define the shape of the action potential in cardiac and smooth muscle. CaV1.2 is inhibited by the action of STIM1.


Human Protein:
UniProt Q13936

Heart, brain, lymphocytes, prostate, bladder, uterus ,stomach, colon, placenta, adrenal gland

Function/ Application:
Ca2+ entry in excitable cells

Arterial hypertension, Long QT syndrome, schizophrenia, Timothy syndrome, BRGDA3, bipolar disorder, schizophrenia

Kir/Gem, CSN5/Jab1, β1-4 subunits, α2δ subunits, NF-κB, osteoprotegerin

Verapamil, nifedipine, kurtoxin, calcicludine, mibefradil, calciseptine, BAYK-8644, verapamil

Patch Clamp: whole cell, room temperature

CaV channels often show a rundown phenomenon. Adequate intra- and extrcellular solutions are essential for a good data quality.

Recommended Reviews:
Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (2005). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels". Pharmacol Rev. 57 (4): 411–25.

Data and Applications

Application Notes


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