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AB191038

Anti-CaV1.3 antibody - C-terminal

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(2 Publications)

Rabbit Polyclonal CaV1.3 antibody. C-terminal. Suitable for WB and reacts with Rat samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human CACNA1D aa 2100 to C-terminus.

View Alternative Names

CACH3, CACN4, CACNL1A2, CCHL1A2, CACNA1D, Voltage-dependent L-type calcium channel subunit alpha-1D, Voltage-gated calcium channel subunit alpha Cav1.3

1 Images
Western blot - Anti-CaV1.3 antibody - C-terminal (AB191038)
  • WB

Supplier Data

Western blot - Anti-CaV1.3 antibody - C-terminal (AB191038)

All lanes:

Western blot - Anti-CaV1.3 antibody - C-terminal (ab191038) at 0.5 µg/mL

All lanes:

Rat brain tissue lysate at 40 µg

Predicted band size: 245 kDa

Observed band size: 245 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Rat

Applications

WB

applications

Immunogen

Synthetic Peptide within Human CACNA1D aa 2100 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q01668

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
Preservative: 0.025% Sodium azide, 0.025% Thimerosal (merthiolate) Constituents: 2.5% BSA, 0.45% Sodium chloride, 0.1% Disodium hydrogenorthophosphate
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

CaV1.3 also known as CACNA1D is a type of L-type voltage-gated calcium channel. It displays a molecular mass of around 250 kDa. This protein predominantly functions in the central nervous system heart and pancreas. It plays an important role in calcium ion influx which is critical for various physiological processes. CaV1.3 channels like other L-type channels are sensitive to dihydropyridines which are commonly used in antihypertensive therapies.
Biological function summary

CaV1.3 channels contribute to the electrical excitability and signaling in cells. They are involved in muscle contraction neurotransmitter release and gene expression. CaV1.3 is part of a calcium signaling complex that tightly regulates intracellular calcium concentration. It interacts with other cellular components to achieve precise control over calcium-dependent processes which is critical for maintaining cellular homeostasis and function.

Pathways

CaV1.3 channels play significant roles in the excitation-contraction coupling pathway in cardiac muscle cells and the insulin secretion pathway in pancreatic beta cells. Their function is closely related to other voltage-gated calcium channels like CaV1.2 which are also part of the calcium signaling pathway. These channels ensure that physiological functions requiring rapid calcium signaling occur efficiently.

CaV1.3 is linked to various conditions including cardiac arrhythmias and neurodegenerative diseases such as Parkinson's disease. Dysregulation of CaV1.3 expression or function may lead to abnormal calcium signaling. In Parkinson's disease altered CaV1.3 activity affects dopaminergic neurons with potential involvement of alpha-synuclein a protein that aggregates in the disease. Understanding these connections provides insights into potential therapeutic targets.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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, and by benzothiazepines.. Isoform Neuronal-type. 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.. Isoform 3. 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.. Isoform 4. 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.
See full target information CACNA1D

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Stem cell research & therapy 9:86 PubMed29615119

2018

Influence of cholesterol/caveolin-1/caveolae homeostasis on membrane properties and substrate adhesion characteristics of adult human mesenchymal stem cells.

Applications

WB

Species

Unspecified reactive species

Jihee Sohn,Hang Lin,Madalyn Rose Fritch,Rocky S Tuan

PLoS pathogens 13:e1006739 PubMed29216332

2017

Voltage-dependent calcium channel signaling mediates GABAA receptor-induced migratory activation of dendritic cells infected by Toxoplasma gondii.

Applications

WB

Species

Unspecified reactive species

Sachie Kanatani,Jonas M Fuks,Einar B Olafsson,Linda Westermark,Benedict Chambers,Manuel Varas-Godoy,Per Uhlén,Antonio Barragan
View all publications

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