Purified Rabbit Polyclonal Antibody (Pab); Voltage-dependent L-type calcium channel subunit alpha-1F; Voltage-gated calcium channel subunit alpha Cav14; CACNA1F; CACNAF1

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Ig

Rabbit

This CACNA1F antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 743-776 amino acids from the Central region of human CACNA1F.

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-CACNA1F antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).

Neuroscience; Signal Transduction

Western Blot (WB)

WB ~~ 1:2000

All lanes : Anti-CACNA1F Antibody (Center) at 1:2000 dilution
Lane 1: A-673 whole cell lysate
Lane 2: Y79 whole cell lysate

Lysates/proteins at 20 ug per lane.

Secondary
Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution.

Predicted band size : 221 kDa

Blocking/Dilution buffer: 5% NFDM/TBST.

220678

calcium channel, voltage-dependent, L type, alpha 1F subunit

voltage-dependent L-type calcium channel subunit alpha-1F

Voltage-dependent L-type calcium channel subunit alpha-1F

CACNAF1??[Similar Products]

CAC1F_HUMAN

This gene encodes a multipass transmembrane protein that functions as an alpha-1 subunit of the voltage-dependent calcium channel, which mediates the influx of calcium ions into the cell. The encoded protein forms a complex of alpha-1, alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Mutations in this gene can cause X-linked eye disorders, including congenital stationary night blindness type 2A, cone-rod dystropy, and Aland Island eye disease. Alternatively spliced transcript variants encoding multiple isoforms have been observed. [provided by RefSeq, Aug 2013]

CACNA1F: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Defects in CACNA1F are the cause of congenital stationary night blindness type 2A (CSNB2A). Congenital stationary night blindness is a non-progressive retinal disorder characterized by impaired night vision. Defects in CACNA1F are the cause of cone-rod dystrophy X- linked type 3 (CORDX3). CORDs are inherited retinal dystrophies belonging to the group of pigmentary retinopathies. CORDs are characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. Defects in CACNA1F are the cause of Aaland island eye disease (AIED); also known as Forsius-Eriksson type ocular albinism. On the Aaland island in the Baltic Sea, AIED is an X-linked recessive retinal disease characterized by a combination of fundus hypopigmentation, decreased visual acuity due to foveal hypoplasia, nystagmus, astigmatism, protan color vision defect, myopia, and defective dark adaptation. Except for progression of axial myopia, the disease can be considered to be a stationary condition. Electroretinography reveals abnormalities in both photopic and scotopic functions. Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1F subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, integral; Membrane protein, multi-pass

Chromosomal Location of Human Ortholog: Xp11.23

Cellular Component: integral to membrane; plasma membrane; voltage-gated calcium channel complex

Molecular Function: voltage-gated calcium channel activity; metal ion binding; high voltage-gated calcium channel activity

Biological Process: cellular calcium ion homeostasis; axonogenesis; visual perception; retina development in camera-type eye; regulation of T cell receptor signaling pathway; dendrite morphogenesis; calcium ion transport; detection of light stimulus involved in visual perception; T cell homeostasis

Disease: Night Blindness, Congenital Stationary, Type 2a; Aland Island Eye Disease; Cone-rod Dystrophy, X-linked, 3

Strom T.M.,et al.Nat. Genet. 19:260-263(1998). Bech-Hansen N.T.,et al.Nat. Genet. 19:264-267(1998). Naylor M.J.,et al.Genomics 66:324-327(2000). Sinnegger-Brauns M.J.,et al.Mol. Pharmacol. 75:407-414(2009). Ross M.T.,et al.Nature 434:325-337(2005).

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