推荐产品
生物源
chicken gizzard
化驗
~80% α-actinin basis (SDS-PAGE)
形狀
ammonium sulfate suspension
分子量
100 kDa
儲存溫度
2-8°C
基因資訊
chicken ... ACTN2(396263) , ACTN4(396024) , RCJMB04_23c5(373918)
human ... ACTN1(87)
mouse ... ACTN1(109711)
rat ... ACTN1(81634)
一般說明
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.
應用
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
生化／生理作用
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.
包裝
Package size based on protein content
外觀
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
準備報告
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).
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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The Journal of physiology, 588(Pt 24), 5105-5114 (2010-10-27)
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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
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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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