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Key Documents

C3868

Sigma-Aldrich

Anti-Calsequestrin-2 antibody produced in rabbit

enhanced validation

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-CASQ2, Anti-fast-twitch, cardiac muscle Calsequestrin

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.44

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~55 kDa

Espèces réactives

rat, human

Réactivité de l'espèce (prédite par homologie)

mouse

Validation améliorée

recombinant expression
Learn more about Antibody Enhanced Validation

Concentration

~1.0 mg/mL

Technique(s)

western blot: 0.5-1.0 μg/mL using HEK-293T cells expressing human calsequestrin-2
western blot: 0.5-1.0 μg/mL using extract of rat cardiac muscle (S1 fraction)

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CASQ2(845)
mouse ... Casq2(12373)
rat ... Casq2(29209)

Description générale

Calsequestrin is a major Ca2+ binding protein in cardiac and skeletal muscle.
Calsequestrin-2 (55 kDa) is found in both sarcoplasmic reticulum′s (SR) terminal cisternae luminal space of both cardiac and in slow skeletal muscle cells. It is made of three domains each with negatively charged thioredoxin-like folds with a β-sheet surrounded by four α-helices.

Immunogène

synthetic peptide corresponding to amino acids 57-74 of rat calsequestrin-2, conjugated to KLH. This sequence is highly conserved in human and rat calsequestrin-2 (single amino acid substitution). This sequence is not found in calsequestrin-1.

Application

Anti-Calsequestrin-2 antibody has been used in immunoblotting, western blotting.
Anti-Calsequestrin-2 is suitable for western blot at a concentration of 0.5-1.0μg/mL using HEK-293T cells expressing human calsequestrin-2 and western blot at a concentration of 0.5-1.0μg/mL using extract of rat cardiac muscle (S1 fraction)

Actions biochimiques/physiologiques

Over expression of cardiac calsequestrin (CASQ2) is associated with depressed cardiovascular function and hypertrophy. Mutations in CASQ2 are thought to be associated with catecholaminergic polymorphic ventricular tachycardia (CPVT). It is a high-capacity, low-affinity Ca2+ binding glycoprotein, which functions as an internal Ca2+ store in the lumen of the sarcoplasmic reticulum (SR).

Forme physique

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Absence of calsequestrin 2 causes severe forms of catecholaminergic polymorphic ventricular tachycardia
Postma A V, et al.
Circulation Research, 91(8), e21-e26 (2002)
Calsequestrin 2 and arrhythmias
Faggioni M and Knollmann B C.
American Journal of Physiology. Heart and Circulatory Physiology, 302(6), H1250-H1260 (2011)
Kathy Ye Morgan et al.
Tissue engineering. Part A, 20(11-12), 1654-1667 (2014-01-15)
Electrical and mechanical stimulation have both been used extensively to improve the function of cardiac engineered tissue as each of these stimuli is present in the physical environment during normal development in vivo. However, to date, there has been no
D H MacLennan et al.
Proceedings of the National Academy of Sciences of the United States of America, 68(6), 1231-1235 (1971-06-01)
An acidic protein has been extracted from sarcoplasmic reticulum with KCl and deoxycholate. The protein, which remains soluble after extraction, has been highly purified by fractionation on DEAE-cellulose, Sephadex, and hydroxylaptite. It has a molecular weight of 44,000 and contains
Calsequestrins in skeletal and cardiac muscle from adult Danio rerio
Furlan S, et al.
Journal of Muscle Research and Cell Motility, 37(1-2), 27-39 (2016)

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