Anti-CaV1.1 (CACNA1S) (extracellular) Antibody

Voltage-gated Ca²⁺ channels (VGCCs) serve as key transducers coupling changes in cell surface membrane potential with local intracellular Ca²⁺ pathways. Among the three families of VGCCs, L-type Ca²⁺ channels (L-VGCCs), include four different isoforms of the α1 pore-forming subunit: Ca_V1.1, Ca_V1.2, Ca_V1.3 and Ca_V1.4¹.
 
Ca_V1.1 (α1S) is the prototypical VGCCs. It was the first member of the Ca_V family to be cloned². Ca_V1.1 is a single polypeptide composed of four relatively conserved repeats (I, II, II and IV) containing six α-helices a piece. The fourth α-helix of each repeat has a regularly spaced sequence of basic residues that is believed to be critical for voltage-sensing. The I–II-linker is the site of interaction with the intracellular β1a subunit ³.
 
Ca_V1.1 is expressed solely in skeletal muscle. It is localized in regions of the T-tubular membrane that are closely opposed to the sarcoplasmic reticulum (the TSR junction).  The primary role of Ca_V1.1 is to serve as the voltage sensor for skeletal muscle-type excitation contraction (EC) coupling⁴.
 
Mutations in Ca_V1.1 have been identified as causative for two congenital muscle pathophysiologies: hypokalemic periodic paralysis⁵ (HypoKPP) and malignant hyperthermia⁶.