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Key Documents

A5044

Sigma-Aldrich

Monoclonal Anti-α-Actinin antibody produced in mouse

clone BM-75.2, ascites fluid

Synonyme(s) :

Anti-BDPLT15

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

BM-75.2, monoclonal

Poids mol.

antigen 100 kDa

Contient

15 mM sodium azide

Espèces réactives

mouse, bovine, human, chicken

Technique(s)

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

Isotype

IgM

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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

Application

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.

Actions biochimiques/physiologiques

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.

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

10 - 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)

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Consulter la Bibliothèque de documents

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
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
Zongwen Tian et al.
PloS one, 9(6), e100715-e100715 (2014-06-25)
Intracellular protein degradation is primarily performed by the ubiquitin-proteasome system (UPS) and the autophagic-lysosomal pathway (ALP). The interplay between these two pathways has been rarely examined in intact animals and the mechanism underlying the interplay remains unclear. Hence, we sought

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