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Key Documents

SAB4503474

Sigma-Aldrich

Anti-Actinin α antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

α-actinin skeletal muscle isoform 2, α-actinin-2, α-actinin-3, ACTN2, F-actin cross-linking protein

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

100

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 103 kDa

Espèces réactives

human, rat, mouse

Concentration

~1 mg/mL

Technique(s)

ELISA: 1:20000
immunofluorescence: 1:100-1:500
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

Numéro d'accès NCBI

P35609

Numéro d'accès UniProt

P35609

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ACTN2(88)

Catégories apparentées

Description générale

Anti-Actinin α Antibody detects endogenous levels of total Actinin α protein.
α-actinin-2 (ACTN2) is a myofibrillar protein that is expressed in cardiac muscle. It is located at the the Z disk. The ACTN2 gene is mapped to human chromosome 1q43.

Immunogène

The antiserum was produced against synthesized peptide derived from human Actinin alpha-2/3.

Immunogen Range: 31-80

Actions biochimiques/physiologiques

Mutation in the α-actinin-2 (ACTN2) gene leads to hypertrophic cardiomyopathy. It is essential in cross-linking actin and titin filaments in the Z-disc. ACTN2 is associated with a number of cytoskeletal and signaling molecules and is involved in the structural and modulatory roles in the organization of the cytoskeleton and muscle contraction.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Chang Yoon Doh et al.
Biochimica et biophysica acta. Molecular basis of disease, 1865(3), 661-677 (2019-01-07)
Mutations in cardiac myosin binding protein C (cMyBPC) are a major cause of hypertrophic cardiomyopathy (HCM). In particular, a single amino acid substitution of tyrosine to serine at residue 237 in humans (residue 235 in mice) has been linked to
Clinical utility gene card for: dilated cardiomyopathy (CMD).
Posafalvi A, et al.
European Journal of Human Genetics, 21(10) (2013)
Katherine L Dominic et al.
The Journal of general physiology, 155(6) (2023-04-18)
Cardiac myosin binding protein C (cMyBPC) is an 11-domain sarcomeric protein (C0-C10) integral to cardiac muscle regulation. In vitro studies have demonstrated potential functional roles for regions beyond the N-terminus. However, the in vivo contributions of these domains are mostly
Jiayang Li et al.
JCI insight, 5(17) (2020-08-05)
Decreased cardiac myosin-binding protein C (cMyBPC) expression due to inheritable mutations is thought to contribute to the hypertrophic cardiomyopathy (HCM) phenotype, suggesting that increasing cMyBPC content is of therapeutic benefit. In vitro assays show that cMyBPC N-terminal domains (NTDs) contain
Hypertrophic cardiomyopathy mutations in the calponin-homology domain of ACTN2 affect actin binding and cardiomyocyte Z-disc incorporation.
Haywood N, et al.
The Biochemical Journal, 473(16), 2485?2493-2485?2493 (2016)
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