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C5988

Sigma-Aldrich

Anti-Calcium Channel (β1 subunit) antibody produced in rabbit

~1 mg/mL, fractionated antiserum, buffered aqueous solution

Synonym(e):

Anti-Voltage-dependent L-type calcium channel, β1 subunit

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About This Item

MDL-Nummer:
MFCD01633054
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

200

Konjugat

unconjugated

Antikörperform

fractionated antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Speziesreaktivität

rat, mouse, human

Konzentration

~1 mg/mL

Methode(n)

western blot: 5-10 μg/mL using rat brain tissue lysate

UniProt-Hinterlegungsnummer

Q02641

Versandbedingung

wet ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... CACNB1(782)
mouse ... Cacnb1(12295)
rat ... Cacnb1(50688)

Allgemeine Beschreibung

The gene CACNB1 (Calcium channel voltage-dependent subunit β 1) is mapped to human chromosome 17q11.2-q22.

Immunogen

synthetic peptide derived from the rat β1 calcium channel conjugated to KLH.

Anwendung

Anti-Calcium Channel (β1 subunit) antibody produced in rabbit is suitable for western blot at a concentration of 5-10 μg/mL using rat brain tissue lysate

Biochem./physiol. Wirkung

The CACNB1 (Calcium channel voltage-dependent subunit β 1) is an intracellular regulatory subunit of voltage-activated calcium channels that has significant impact on membrane expression and electrophysical characteristics of the channel. Calcium channel β subunits regulate voltage-dependent calcium currents through direct interaction with α1 subunits. CACNB1 is a target of miRNA-328. In mouse model, CACNB1 is involved in gene expression in muscle progenitor cells and regulates skeletal muscle mass during embryonic development by suppressing myogenin.

Physikalische Form

Solution in phosphate buffered saline containing 0.08% sodium azide.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Analysenzertifikate (COA)

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Jackson Taylor et al.
The Journal of cell biology, 205(6), 829-846 (2014-06-18)
Voltage-gated calcium channel (Cav) β subunits are auxiliary subunits to Cavs. Recent reports show Cavβ subunits may enter the nucleus and suggest a role in transcriptional regulation, but the physiological relevance of this localization remains unclear. We sought to define
Yanjie Lu et al.
Circulation, 122(23), 2378-2387 (2010-11-26)
A characteristic of both clinical and experimental atrial fibrillation (AF) is atrial electric remodeling associated with profound reduction of L-type Ca(2+) current and shortening of the action potential duration. The possibility that microRNAs (miRNAs) may be involved in this process
R G Gregg et al.
Genomics, 15(1), 185-187 (1993-01-01)
A human clone containing a portion of the gene encoding several isoforms of the beta 1 subunit of voltage-dependent calcium channels was isolated and partially sequenced. The gene was mapped to chromosome 17 using the polymerase chain reaction with oligonucleotides
Solmaz Etemad et al.
Channels (Austin, Tex.), 8(4), 334-343 (2014-05-31)
Voltage-gated calcium channels regulate gene expression by controlling calcium entry through the plasma membrane and by direct interactions of channel fragments and auxiliary β subunits with promoters and the epigenetic machinery in the nucleus. Mutations of the calcium channel β(4)
Xingfu Xu et al.
The Journal of biological chemistry, 286(11), 9677-9687 (2011-01-12)
The β subunits of voltage-gated Ca(2+) channels are best known for their roles in regulating surface expression and gating of voltage-gated Ca(2+) channel α(1) subunits. Recent evidence, however, indicates that these proteins have a variety of Ca(2+) channel-independent functions. For

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