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Anti-Cav1.1 alpha1s Antibody, clone 1A, Ascites Free clone 1A, from mouse

ITEM#: 3042-MAB427C

MFR#: MAB427-C

Voltage-dependent L-type calcium channel subunit alpha-1S (UniProt P07293; also known as Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle, Voltage-gated calcium channel subunit alpha Cav1.1) is encoded by the CACNA1S (also kno

Voltage-dependent L-type calcium channel subunit alpha-1S (UniProt P07293; also known as Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle, Voltage-gated calcium channel subunit alpha Cav1.1) is encoded by the CACNA1S (also known as CACH1, CACN1, CACNL1A3) gene (Gene ID 100009585) in Oryctolagus cuniculus (rabbit) species. Voltage-dependent calcium channels (VDCC) are found in the membrane of excitable cells (e.g., muscle, glial cells, neurons) and exhibit 1000-fold greater permeability to calcium than to sodium under normal physiological conditions. There exist five types of VDCCs, including four high voltage-activated channels (Neural- or N-type channel, Residual- or R-type channel, Purkinje- or P/Q-type channel, and the dihydropyridine-sensitive Long-lasting or L-type channels) and the low voltage-activated Transient or T-type calcium channels. VDCCs exist as a complex of different subunits (alpha1, alpha2delta, beta1-4, and gamma), with alpha1 being the the ion-conducting pore-forming subunit that contains voltage-sensing machinery and the drug/toxin-binding sites. There exist ten genes coding for different alpha1 subunits, four of which code for L-type alpha-1 subunits (alpha-1A/Cav2.1/CACNA1A, alpha-1C/Cav1.2/CACNA1C, alpha-1D/Cav1.3/CACNA1D, and alpha-1S/Cav1.1/CACNA1S). The dihydropyridine-sensitive L-type channels are responsible for excitation-contraction coupling of skeletal, smooth, and cardiac muscle and for hormone secretion in endocrine cells. The alpha1S subunit (Cav1.1) contains the characteristic four homologous I-IV domains (a.a. 38-337, 418-664, 786-1068, 1105-1384) with six transmembrane alpha-helices each, having both its N- and C-terminal ends exposed intracellularly (a.a. 1-51, 1382-1873).