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CACNA1D antibody (Calcium Channel, Voltage-Dependent, L Type, alpha 1D Subunit) (AA 700-800)

Details for Product anti-CACNA1D Antibody No. ABIN350138, Supplier: Log in to see
Antigen
  • 8430418G19Rik
  • C79217
  • ca(v)1.3
  • CACH3
  • CACN4
  • cacna1d
  • Cacnl1a2
  • CACNL1A2
  • cav1.3
  • Cav1.3
  • cav1.3a
  • Cchl1a
  • Cchl1a2
  • CCHL1A2
  • D-LTCC
  • isl
  • SANDD
  • si:dz136d19.3
  • si:dz223c6.1
Epitope
AA 700-800
41
37
13
3
3
2
2
1
1
1
1
Reactivity
Human, Rat (Rattus), Mouse (Murine)
116
78
74
4
Host
Rabbit
96
29
Clonality
Polyclonal
Conjugate
This CACNA1D antibody is un-conjugated
5
5
5
5
4
4
4
4
4
4
4
4
4
4
4
4
3
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
111
92
87
86
69
15
11
6
4
3
2
1
Supplier
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Supplier Product No.
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Immunogen A synthetic peptide from aa region 700-800 of human CACNA1D (Cav1.3) conjugated to an immunogenic carrier protein was used as the antigen.
Specificity Specific for CACNA1D.
Purification Whole serum
Alternative Name CACNA1D (CACNA1D Antibody Abstract)
Background Function: 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-1D 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).
Subcellular location: Membrane, Multi-pass membrane protein.
Tissue specificity: Expressed in pancreatic islets and in brain, where it has been seen in hippocampus, basal ganglia, habenula and thalamus. No expression in skeletal muscle. Also known as: Voltage-dependent L-type calcium channel subunit alpha-1D, Voltage-gated calcium channel subunit alpha Cav1.3, Calcium channel, L type, alpha-1 polypeptide, CACH3, CACN4, CACNL1A2, CCHL1A2, Cav3.1.
Application Notes A dilution of 1 : 300 to 1 : 2000 is recommended.
The optimal dilution should be determined by the end user. Not tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Olsen, Blagoev, Gnad, Macek, Kumar, Mortensen, Mann: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Kamp, Mitas, Fields, Asoh, Chin, Marban, Nirenberg: "Transcriptional regulation of the neuronal L-type calcium channel alpha 1D subunit gene." in: Cellular and molecular neurobiology, Vol. 15, Issue 3, pp. 307-26, 1995 (PubMed).

Yamada, Masuda, Li, Ihara, Kubota, Miura, Nakamura, Fujii, Seino, Seino: "The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes." in: Genomics, Vol. 27, Issue 2, pp. 312-9, 1995 (PubMed).

Seino, Chen, Seino, Blondel, Takeda, Johnson, Bell: "Cloning of the alpha 1 subunit of a voltage-dependent calcium channel expressed in pancreatic beta cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 2, pp. 584-8, 1992 (PubMed).

Williams, Feldman, McCue, Brenner, Velicelebi, Ellis, Harpold: "Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype." in: Neuron, Vol. 8, Issue 1, pp. 71-84, 1992 (PubMed).