A9776
α-Actinin from chicken gizzard
~80% α-actinin basis (SDS-PAGE), ammonium sulfate suspension
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 Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
动植物来源生物产品
常规特殊物品
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Meishan Li et al.
Aging cell, 14(2), 228-235 (2015-02-04)
Novel experimental methods, including a modified single fiber in vitro motility assay, X-ray diffraction experiments, and mass spectrometry analyses, have been performed to unravel the molecular events underlying the aging-related impairment in human skeletal muscle function at the motor protein
Wiebke Onkes et al.
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
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
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
Flavius C Pascut et al.
Biochimica et biophysica acta, 1830(6), 3517-3524 (2013-02-14)
Online label-free monitoring of in-vitro differentiation of stem cells remains a major challenge in stem cell research. In this paper we report the use of Raman micro-spectroscopy (RMS) to measure time- and spatially-resolved molecular changes in intact embryoid bodies (EBs)
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