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.
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.
Biochem/physiol Actions
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.
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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
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
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
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
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