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A7811

Sigma-Aldrich

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

clone EA-53, ascites fluid

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Synonym(s):
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
MDL number:
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

EA-53, monoclonal

mol wt

antigen 100 kDa

contains

15 mM sodium azide

species reactivity

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

technique(s)

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

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Specificity

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).

Immunogen

Rabbit skeletal α-actinin

Application

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.

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

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.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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)
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)
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)
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)
Expression of the erythropoietin receptor in human heart.
Depping R, et al.
The Journal of Thoracic and Cardiovascular Surgery, 130(3), 877-e19-877-e19 (2005)

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