CACNA1C / Cav1.2 Antibody (C-Terminus)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P |
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Primary Accession | Q13936 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Calculated MW | 249kDa |
Dilution | IHC-P (5 µg/ml) |
Gene ID | 775 |
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Other Names | Voltage-dependent L-type calcium channel subunit alpha-1C, Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle, Voltage-gated calcium channel subunit alpha Cav1.2, CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1 |
Target/Specificity | Human CACNA1C / Cav1.2. BLAST analysis of the peptide immunogen showed no homology with other human proteins. |
Reconstitution & Storage | Long term: -70°C; Short term: +4°C |
Precautions | CACNA1C / Cav1.2 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | CACNA1C |
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Synonyms | CACH2, CACN2, CACNL1A1, CCHL1A1 |
Function | Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:8392192, PubMed:7737988, PubMed:9087614, PubMed:9013606, PubMed:9607315, PubMed:12176756, PubMed:17071743, PubMed:11741969, PubMed:8099908, PubMed:12181424, PubMed:29078335, PubMed:29742403, PubMed:16299511, PubMed:20953164, PubMed:15454078, PubMed:15863612, PubMed:17224476, PubMed:24728418, PubMed:26253506, PubMed:27218670, PubMed:23677916, PubMed:30023270, PubMed:30172029, PubMed:34163037). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:15454078, PubMed:15863612, PubMed:17224476, PubMed:24728418, PubMed:26253506). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable). |
Cellular Location | Cell membrane; Multi-pass membrane protein Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q01815}. Note=Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. {ECO:0000250|UniProtKB:P15381} |
Tissue Location | Detected throughout the brain, including hippocampus, cerebellum and amygdala, throughout the heart and vascular system, including ductus arteriosus, in urinary bladder, and in retina and sclera in the eye (PubMed:15454078). Expressed in brain, heart, jejunum, ovary, pancreatic beta-cells and vascular smooth muscle Overall expression is reduced in atherosclerotic vascular smooth muscle. |
Volume | 50 µl |
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Background
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-1C 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). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.
References
Soldatov N.M.,et al.Proc. Natl. Acad. Sci. U.S.A. 89:4628-4632(1992).
Schultz D.,et al.Proc. Natl. Acad. Sci. U.S.A. 90:6228-6232(1993).
Soldatov N.M.,et al.Genomics 22:77-87(1994).
Soldatov N.M.,et al.J. Biol. Chem. 270:10540-10543(1995).
Kloeckner U.,et al.Am. J. Physiol. 272:H1372-H1381(1997).
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