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Key Documents

A9776

Sigma-Aldrich

α-Actinin from chicken gizzard

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

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About This Item

Número de CAS:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

chicken gizzard

assay

~80% α-actinin basis (SDS-PAGE)

form

ammonium sulfate suspension

mol wt

100 kDa

storage temp.

2-8°C

Gene Information

General description

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.

Application

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 Actions

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.

Packaging

Package size based on protein content

Physical 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

Preparation Note

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).

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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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
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
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Genes, chromosomes & cancer, 52(5), 512-522 (2013-01-31)
About 20% of ovarian carcinomas show alterations of 19p13 and/or 19q13 in the form of added extra material whose origin often is from chromosome 11. Based on earlier spectral karyotype analysis of the ovarian cancer cell line SKOV-3, which shows
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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
Meishan Li et al.
The Journal of physiology, 588(Pt 24), 5105-5114 (2010-10-27)
Muscle, motor unit and muscle fibre type-specific differences in force-generating capacity have been investigated for many years, but there is still no consensus regarding specific differences between slow- and fast-twitch muscles, motor units or muscle fibres. This is probably related

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