A9776
α-Actinin from chicken gizzard
~80% α-actinin basis (SDS-PAGE), ammonium sulfate suspension
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About This Item
Form:
ammonium sulfate suspension
Assay:
~80% α-actinin basis (SDS-PAGE)
Biological source:
chicken gizzard
Mol wt:
100 kDa
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
chicken ... ACTN2(396263), ACTN4(396024), RCJMB04_23c5(373918)
human ... ACTN1(87)
mouse ... ACTN1(109711)
rat ... ACTN1(81634)
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).
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
动植物来源生物产品
常规特殊物品
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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
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
Norman Y Yao et al.
Physical review letters, 110(1), 018103-018103 (2013-02-07)
A hallmark of biopolymer networks is their sensitivity to stress, reflected by pronounced nonlinear elastic stiffening. Here, we demonstrate a distinct dynamical nonlinearity in biopolymer networks consisting of filamentous actin cross-linked by α-actinin-4. Applied stress delays the onset of relaxation
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
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