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Key Documents

SAB4503474

Sigma-Aldrich

Anti-Actinin α antibody produced in rabbit

affinity isolated antibody

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 103 kDa

species reactivity

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

NCBI accession no.

P35609

UniProt accession no.

P35609

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ACTN2(88)

Related Categories

General description

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.

Immunogen

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

Immunogen Range: 31-80

Biochem/physiol Actions

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.

Features and Benefits

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.

Physical form

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

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

12 - Non Combustible Liquids

WGK

nwg

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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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)
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
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