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Merck

A5044

Sigma-Aldrich

Monoclonal Anti-α-Actinin antibody produced in mouse

clone BM-75.2, ascites fluid

Synonym(e):

Anti-BDPLT15

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

ascites fluid

Antikörper-Produkttyp

primary antibodies

Klon

BM-75.2, monoclonal

Mol-Gew.

antigen 100 kDa

Enthält

15 mM sodium azide

Speziesreaktivität

mouse, bovine, human, chicken

Methode(n)

indirect immunofluorescence: 1:200 using cultured chicken fibroblasts
microarray: suitable
western blot: suitable

Isotyp

IgM

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... ACTN1(87)
mouse ... Actn1(109711)

Allgemeine Beschreibung

α-actinin is a 100kD actin binding protein found in muscle as well as non-muscle cells. In smooth muscle, α-actinin is identified in dense bodies and plaques characteristic of tissues whereas it is associated with z-discs that define muscle sarcomas in normal skeletal muscle. Monoclonal anti-α-actinin antibody can be used in immunoblotting to study the membrane anchorage sites and immunochemical identification of α-actinin. It can also be used in immunofluorescence to study the localization of α-actinin in cultured cells and tissues. Mouse anti-α-actinin antibody reacts specifically with chicken fibroblasts. The product has also shown reactivity for mouse and human cells.
The gene encoding α-actinin is mapped to the human chromosome 11q13.2. α-actinin belongs to the spectrin protein superfamily.

Immunogen

cytoskeletal fraction of bovine mammary gland epithelial (BMGE) cells.

Anwendung

Immunofluorescence of cardiomyocytes from neonatal and adult mouse hearts was performed using monoclonal mouse anti-α actinin (clone EA-53) at 1:1000.
May be used in the study of skeletal muscle organization and in studies of the membrane anchorage sites of actin.
Monoclonal anti-α-actinin antibody (diluted 1: 500) can be used in native protein binding assays. It can also be used in western blot, microarray, immunohistochemistry and in Immunofluorescence microscopy.

Biochem./physiol. Wirkung

α−actinin regulates muscle contraction and cytoskeletal organization. It promotes cell migration and acts as an actin crosslinker. Mutations in the α-actinin gene is observed in heterogeneous hypertrophic cardiomyopathy and in juvenile onset atrial fibrillation.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

C A Conley
American journal of physiology. Cell physiology, 280(6), C1645-C1656 (2001-05-15)
Evidence is accumulating to suggest that actin filament remodeling is critical for smooth muscle contraction, which implicates actin filament ends as important sites for regulation of contraction. Tropomodulin (Tmod) and smooth muscle leiomodin (SM-Lmod) have been found in many tissues
Protein Interactions with the Glucose Transporter Binding Protein GLUT1CBP That Provide a Link between GLUT1 and the Cytoskeleton.
Robert C. Bunn, Mari Anne Jensen
Molecular and Cellular Biology, 10(4), 819-832 (1999)
Thomas A Hawkins et al.
Development (Cambridge, England), 135(6), 1147-1156 (2008-02-08)
The mechanisms that regulate sarcomere assembly during myofibril formation are poorly understood. In this study, we characterise the zebrafish sloth(u45) mutant, in which the initial steps in sarcomere assembly take place, but thick filaments are absent and filamentous I-Z-I brushes
C M Laukaitis et al.
The Journal of cell biology, 153(7), 1427-1440 (2001-06-27)
To investigate the mechanisms by which adhesions form and disperse in migrating cells, we expressed alpha 5 integrin, alpha-actinin, and paxillin as green fluorescent protein (GFP) fusions. All localized with their endogenous counterparts and did not perturb migration when expressed
Novel α-actinin 2 variant associated with familial hypertrophic cardiomyopathy and juvenile atrial arrhythmias: a massively parallel sequencing study
Girolami F, et al.
Circulation: Genomic and Precision Medicine, 7(6), 741-750 (2014)

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