Anti-CavY1

Antibodies

CaVγ1, CACNLG, Voltage-dependent calcium channel gamma-1 subunit, Dihydropyridine-sensitive L-type, skeletal muscle Ca2+ channel subunit gamma

Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C

Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4

CaVγ1, CACNLG, Voltage-dependent calcium channel gamma-1 subunit, Dihydropyridine-sensitive L-type, skeletal muscle Ca2+ channel subunit gamma - A Rabbit Polyclonal Antibody to CACNG1 (CaVγ1) Subunit

Mouse - identical; human - 13/14 amino acid residues identical

Confirmed by amino acid analysis and mass spectrometry

0.8 mg/ml

1st extracellular loop

Rat

41116161

Voltage-gated Ca2+ (CaV) channels are ubiquitously expressed and function as Ca2+conducting pores in the plasma membrane1. On the basis of their voltage activation properties, the voltage-gated Ca2+ channels can be further divided into two broad groups: the low (T-type) and high (L, N, P, Q and R-type) threshold-activated channels.2. CaV channels are heteromultimers composed of four independently encoded proteins, the pore-forming α1 subunit, which triggers Ca2+ flow across the membrane, and the auxiliary subunits α2δ, γ, and β3.CaVγ subunits inhibit CaV channel activity and modulate its activation and inactivation kinetics. CaVγ subunits have little effect on CaV channel trafficking4. The γ subunit is an integral membrane protein. The γ subunit family consists of at least 8 members, which share a number of common structural features. Each member is predicted to possess four transmembrane domains, with intracellular N- and C-termini. The first extracellular loop contains a highly conserved N-glycosylation site and a pair of conserved cysteine residues5.CaVγ1 is solely expressed in skeletal muscle and associates with the α1S (CaV1.1) subunit6.Knockout mice are indeed viable and show no extreme phenotype. It seems that γ1 enhances the inactivation of ER Ca2+ release in a voltage-dependent manner6.