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Merck

A9776

Sigma-Aldrich

α-Actinin aus Hühner-Muskelmagen

~80% α-actinin basis (SDS-PAGE), ammonium sulfate suspension

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About This Item

CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.32

Biologische Quelle

chicken gizzard

Assay

~80% α-actinin basis (SDS-PAGE)

Form

ammonium sulfate suspension

Mol-Gew.

100 kDa

UniProt-Hinterlegungsnummer

Lagertemp.

2-8°C

Angaben zum Gen

Allgemeine Beschreibung

α-Actinin exists as a rod-shaped antiparallel dimer with two elongated subunits. The domain region contains an N-terminal actin-binding domain with tandem calponin homology domains, a central tandem 3-helix motifs, and EF-hand motifs at C-terminus. It belongs to the spectrin superfamily and is localized in actin structures.

Anwendung

α-Actinin from chicken gizzard has been used:
  • as an antigen to coat plates for the capture of anti-actinin antibody using enzyme-linked immunosorbent assay (ELISA) from tumor cell line clones
  • in in vitro motility experiments to test its effect on actin filament movement
  • to coat cantilevers for strengthening fluorescently labeled actin filaments in force measurement studies

Biochem./physiol. Wirkung

α-Actinin binds actin and has the ability to crosslink actin cytoskeleton. It also plays a key role in the structural maintenance of the Z-disk of striated muscle.

Verpackung

Package size based on protein content

Physikalische Form

Suspension in 2 M (NH4)2SO4 containing 20 mM Tris acetate, pH 7.6, 20 mM sodium chloride, 0.1 mM EDTA, 15 mM β-mercaptoethanol and 1 mM phenylmethylsulfonyl fluoride

Angaben zur Herstellung

Alpha-actinin ammonium sulfate suspension should be mixed sufficiently and further diluted prior to use. Protein precipitate will be present in solution with high protein concentrations.

Prepared using a modification of the procedure of Neidel, J.E. and Cuatrecasas, P., Biochem. Biophys. Res. Commun., 91, 152 (1979).

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

F Rivero et al.
Journal of cell science, 112 ( Pt 16), 2737-2751 (1999-07-22)
The contribution of three actin cross-linking proteins, alpha-actinin (alphaA), gelation factor (ABP-120), and the 34 kDa actin-bundling protein to cellular functions has been studied in three single mutant (alphaA-, 120-, and 34-) and three double mutant (alphaA-/120-, 34-/alphaA-, 34-/120-) strains
Anja Katzemich et al.
PLoS genetics, 9(3), e1003342-e1003342 (2013-03-19)
The Drosophila Alp/Enigma family protein Zasp52 localizes to myotendinous junctions and Z-discs. It is required for terminal muscle differentiation and muscle attachment. Its vertebrate ortholog ZASP/Cypher also localizes to Z-discs, interacts with α-actinin through its PDZ domain, and is involved
Jun Liu et al.
Journal of molecular biology, 338(1), 115-125 (2004-03-31)
Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays of smooth muscle alpha-actinin. The reconstruction reveals a well-resolved long central domain with 90 degrees of left-handed twist and near 2-fold symmetry. However, the
Timothy Travers et al.
Biophysical journal, 104(3), 705-715 (2013-02-28)
The assembly of proteins into multidomain complexes is critical for their function. In eukaryotic nonmuscle cells, regulation of the homodimeric actin cross-linking protein α-actinin-4 (ACTN4) during cell migration involves signaling receptors with intrinsic tyrosine kinase activity, yet the underlying molecular
Nicola Cacciani et al.
Acta physiologica (Oxford, England), 229(1), e13425-e13425 (2019-12-05)
Critical illness myopathy (CIM) represents a common consequence of modern intensive care, negatively impacting patient health and significantly increasing health care costs; however, there is no treatment available apart from symptomatic and supportive interventions. The chaperone co-inducer BGP-15 has previously

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