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Key Documents

A7811

Sigma-Aldrich

Monoclonal Anti-α-Actinin (Sarcomeric) antibody produced in mouse

clone EA-53, ascites fluid

Sinonimo/i:

Actinin Antibody, Sarcomeric Alpha Actinin Antibody, Sarcomeric Alpha Actinin Antibody - Monoclonal Anti-α-Actinin (Sarcomeric) antibody produced in mouse, Anti-1110008F24Rik, Anti-ACTN2, Anti-Actinin α2, Anti-CMD1AA, Anti-MGC107582

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

ascites fluid

Tipo di anticorpo

primary antibodies

Clone

EA-53, monoclonal

PM

antigen 100 kDa

contiene

15 mM sodium azide

Reattività contro le specie

mouse, human, frog, pig, feline, chicken, hamster, canine, bovine, fish, snake, rabbit, sheep, goat, rat, lizard

tecniche

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:800 using human skeletal and cardiac muscle
indirect ELISA: suitable using human and animal muscle tissue
indirect immunofluorescence: suitable using human and animal cultured muscle cells
western blot: 1:2,500 using rat leg muscle

Isotipo

IgG1

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... ACTN2(88)
mouse ... Actn2(11472)
rat ... Actn2(291245)

Descrizione generale

α-Actinin (ACTN2) is a 100kDa actin-binding protein that is found in muscle as well as non-muscle cells. In smooth muscles, α-actinin is present in dense bodies and plaques whereas in normal skeletal muscles, it is associated with z-discs that define muscle sarcomeres. ACTN2 is located on human chromosome lq42-q43. α-actinin has rod shaped N-terminal domain.
Mouse monoclonal anti-α-actinin (sarcomeric) antibody stains thymic myoid cells. The antibody exhibits wide reactivity with human and animal muscle tissue.
The antibody is specific for a-skeletal and a-cardiac muscle actinins. The antibody labels Z lines and dots in stress fibers of skeletal muscle in myotubes but does not react with non-skeletal muscle elements (e.g., connective tissue, epithelium, nerves, smooth muscle).
Mouse monoclonal anti-α-actinin (sarcomeric) antibody stains thymic myoid cells. The antibody exhibits wide reactivity with human and animal muscle tissue. α-actinin is detected predominantly in dense bodies and plaques which are characteristic of that tissue. Immunofluorescent labeling of a large variety of cells with anti a -actinin reveals an extensive association of the proteins with the actin containing stress fibers and, in particular, with their membrane-bound termini.
Monoclonal Anti-α-Actinin (Sarcomeric) (mouse IgG1 isotype) is derived from the EA-53 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with purified rabbit skeletal a-actinin.1 The isotype is determined using Mouse Monoclonal Antibody Isotyping Reagents, Catalog Number ISO2. Monoclonal Anti-α-Actinin (Sarcomeric) may be used for the localization of sarcomeric α-actinin using various immunochemical assays such as ELISA, dot blot, immunoblot, immunohistochemistry, and immunocytochemistry. The antibody is useful in the immunolocalization of α-actinin in normal and neoplastic cultured cells and tissues, and for studies on the state of sarcomeric muscle organization, in normal and pathological situations.

Specificità

The antibody is specific for a-skeletal and α-cardiac muscle actinins. The antibody labels Z lines and dots in stress fibers of skeletal muscle in myotubes but does not react with non-skeletal muscle elements (e.g., connective tissue, epithelium, nerves, smooth muscle).

Immunogeno

Rabbit skeletal α-actinin

Applicazioni

Cardiac myocytes were stained with monoclonal mouse anti-actinin to visualize the Z-lines after fixation in pre-cooled methanol/acetone mix (1:1) for 10 minutes at 4 °C.
Mouse monoclonal anti-α-actinin (sarcomeric) antibody is suitable for immunohistochemistry (1:800), ELISA, immunofluorescence and western blot (1:2,500) applications.

Azioni biochim/fisiol

α-actinin functions as an actin crosslinker and promotes cell migration. Mutations in α-actinin gene locus is observed in patients with heterogeneous hypertrophic cardiomyopathy and in juvenile onset atrial fibrillation.

Stato fisico

Supplied as ascites fluid with 15 mM sodium azide as a preservative

Stoccaggio e stabilità

Store at -20 °C. For continuous use, the product may be stored at 2-8 °C for up to one month. For extended storage, the solution may be frozen in working aliquots at -20 °C. Repeated freezing and thawing, or storage in "frost-free" freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

Esclusione di responsabilità

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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N° Catalogo
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Determinazione del prezzo

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11.
Beggs A H, et al.
The Journal of Biological Chemistry, 267(13), 9281-9288 (1992)
MicroRNA-1 and-499 regulate differentiation and proliferation in human-derived cardiomyocyte progenitor cells.
Sluijter J P, et al.
Arteriosclerosis, Thrombosis, and Vascular Biology, 30(4), 859-868 (2010)
T Gao et al.
The Journal of biological chemistry, 272(31), 19401-19407 (1997-08-01)
The properties of cardiac L-type channels have been well characterized electrophysiologically, and many such studies have demonstrated that the channels are regulated by a cAMP-dependent pathway. However, the subunit composition of native cardiac L-type calcium channels has not been completely
Tissue-specific expression and α-actinin binding properties of the Z-disc titin: implications for the nature of vertebrate Z-discs1.
Sorimachi H, et al.
Journal of Molecular Biology, 270(5), 688-695 (1997)
Identification and subcellular localization of the subunits of L-type calcium channels and adenylyl cyclase in cardiac myocytes.
Gao T, et al.
The Journal of Biological Chemistry, 272(31), 19401-19407 (1997)

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High titer lentiviral particles including beta-actin, alpha-tubulin and vimentin used for live cell analysis of cytoskeleton structure proteins.

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