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C5105

Sigma-Aldrich

Anti-Calcium Channel (α2/δ-1 Subunit) antibody produced in rabbit

affinity isolated antibody, lyophilized powder

Synonym(s):

Anti-CACNA2, Anti-CACNL2A, Anti-CCHL2A, Anti-LINC01112, Anti-lncRNA-N3

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.43

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

mouse, rat, pig, human

technique(s)

western blot (chemiluminescent): 1:200 using rat brain membranes

UniProt accession no.

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

CACNA2D1 (calcium channel, voltage-dependent, α2/δ subunit 1) is a member of a family of GPI-anchored voltage-gated calcium channels (VGCCs)-associated subunits called α2δ. VGCC are composed of three types of subunits- pore-forming α1 and auxiliary β and α2δ subunits.

Immunogen

synthetic peptide corresponding to amino acids 1-15 of α2 subunit (amino acids 27-41 of rabbit α2/δ−1 precursor).

Application

Anti-Calcium Channel (α2/δ-1 Subunit) antibody produced in rabbit has been used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

CACNA2D1 (calcium channel, voltage-dependent, α2/δsubunit 1) is a type of α2δs, which are involved in the synaptic neurotransmitter release as they are concentrated at the synapses. They have a chaperone-like activity in non-neuronal cells. This protein acts as a target for gabapentin, which is a neuropathic analgesic. Mutations in this gene, in humans result in short QT syndrome (SQTS).

Target description

L-type of Voltage-gated Ca2+ Channel.

Physical form

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

Preparation Note

Reconstitute the 0.05 mL vial with 50 μL deionized water. Reconstitute the 0.2 mL vial with 0.2 mL deionized water. After reconstitution, the antibody concentration is ~0.8 mg/mL.

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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Macroglia-derived thrombospondin 2 regulates alterations of presynaptic proteins of retinal neurons following elevated hydrostatic pressure
Wang S, et al.
Testing, 12(9), e0185388-e0185388 (2017)
Kjara S Pilch et al.
The Journal of physiology, 600(24), 5333-5351 (2022-11-16)
In the mammalian brain, presynaptic CaV 2 channels play a pivotal role in synaptic transmission by mediating fast neurotransmitter exocytosis via influx of Ca2+ into the active zone of presynaptic terminals. However, the distribution and modulation of CaV 2.2 channels
Transcription Factor Sp1 Regulates the Expression of Calcium Channel $\alpha$2$\delta$-1 Subunit in Neuropathic Pain
Gomez k, et al.
Neuroscience, 12(9), e0185388-e0185388 (2019)
Acute post-injury blockade of I?2I'-1 calcium channel subunits prevents pathological autonomic plasticity after spinal cord injury.
Brennan, et al.
Cell Reports, 34, 108667-108667 (2022)
Yuki Domon et al.
The Journal of pharmacology and experimental therapeutics, 365(3), 573-582 (2018-03-23)
Mirogabalin ([(1R,5S,6S)-6-(aminomethyl)-3-ethylbicyclo[3.2.0]hept-3-en-6-yl]acetic acid), a novel ligand for the α2δ subunit of voltage-gated calcium channels, is being developed to treat pain associated with diabetic peripheral neuropathy and postherpetic neuralgia. In the present study, we investigated the in vitro binding characteristics and

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