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C1868

Sigma-Aldrich

Anti-Calcium Channel CaV3.2 (α1H) antibody produced in rabbit

affinity isolated antibody, lyophilized powder

Synonym(s):

Anti-CACNA1HB, Anti-Cav3.2, Anti-ECA6, Anti-EIG6, Anti-HALD4

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

rat

technique(s)

western blot: 1:200 using lysate from the ND7/23 cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Calcium channel, voltage-dependent, T type, α1H subunit (CACNA1H) is a protein encoded by the CACNA1H gene in humans and is mapped to chromosome 16p13.3. The proteins are membrane protein machinery performing selective permeation of external calcium ions. The α1H channel is sensitive to mibefradil, a nondihydropyridine Ca2+ channel blocker. CACNA1H is abundantly expressed in both peripheral and central endings of the primary afferent neurons, regulating neuronal excitability and release of excitatory neurotransmitters.

Immunogen

synthetic peptide CHVEGPQERARVAHS corresponding to amino acid residues 581-595 of rat CaV3.2. Epitope location: intracellular loop connecting D1-D2. Mouse, bovine, and canine have 14/15 residues identical; human has 13/15 residues identical.

Application

Anti-Calcium Channel CaV3.2 (α1H) antibody produced in rabbit is suitable for western blotting at a dilution of 1:200 using lysate from the ND7/23 cell line.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

Calcium channel, voltage-dependent, T type, α1H subunit (CACNA1H) plays an essential role in regulating neuronal excitability and network oscillations in the brain. Mutations in the gene are associated with various forms of idiopathic generalized epilepsy. Gaining-of-function mutation in CACNA1H increases seizure susceptibility by directly altering neuronal electrical properties and indirectly by changing gene expression. CACNA1H acts as an important mediator of Ca2+ entry near the resting membrane potential. It plays a pivotal role in processing of pain signals and may serve as a novel target for development of drugs for the treatment of intractable pain resistant to currently available analgesics. CACNA1H up-regulation is involved in the pathophysiology of inflammatory, neuropathic and visceral pain.

Physical form

Lyophilized from phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin, and 0.05% sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Despina Tsortouktzidis et al.
Frontiers in molecular neuroscience, 14, 667143-667143 (2022-01-25)
Precise genome editing in combination with viral delivery systems provides a valuable tool for neuroscience research. Traditionally, the role of genes in neuronal circuits has been addressed by overexpression or knock-out/knock-down systems. However, those techniques do not manipulate the endogenous
Hyun-Jee Park et al.
Cell calcium, 54(3), 226-235 (2013-07-16)
Voltage-activated Ca2+ channels are membrane protein machinery performing selective permeation of external calcium ions. The main Ca2+ selective filters of all high-voltage-activated Ca2+ channel isoforms are commonly composed of four Glu residues (EEEE), while those of low-voltage-activated T-type Ca2+ channel
K E Rose et al.
Neuroscience, 250, 263-274 (2013-07-23)
Previous behavioral studies have revealed that CaV3.2 T-type calcium channels support peripheral nociceptive transmission and electrophysiological studies have established the presence of T-currents in putative nociceptive sensory neurons of dorsal root ganglion (DRG). To date, however, the localization pattern of
Fumiko Sekiguchi et al.
Journal of pharmacological sciences, 122(4), 244-250 (2013-08-02)
Low-voltage-activated T-type Ca(2+) channels (T-channels), especially Cav3.2 among the three isoforms (Cav3.1, Cav3.2, and Cav3.3), are now considered to play pivotal roles in processing of pain signals. Cav3.2 T-channels are functionally modulated by extracellular substances such as hydrogen sulfide and
Hem Kumar Tamang et al.
Journal of thrombosis and haemostasis : JTH, 20(8), 1887-1899 (2022-05-02)
Cav 3.2 is a T-type calcium channel that causes low-threshold exocytosis. T-type calcium channel blockers reduce platelet granule exocytosis and aggregation. However, studies of the T-type calcium channel in platelets are lacking. To examine the expression and role of Cav

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