A9776
α-Actinin from chicken gizzard
~80% α-actinin basis (SDS-PAGE), ammonium sulfate suspension
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service