Alpha-Actinin 4 (non-muscle) - 2x50 µg
α-Actinin 4
(non-muscle isoform)
Description
| Protein | α-Actinin 4 (non-muscle) |
| Origin | Murine, recombinant |
| Molecular mass | ~100 kDa per monomer / ~200 kDa per dimer |
| Protein description | α-Actinins belong to the spectrin superfamily and are divided into four isoforms, encoded by different genes. Isoforms 2 and 3 (“muscle” α-actinins) are constituents of sarcomeres in cross-striated skeletal and cardiac muscle. Isoforms 1 and 4 (“non-muscle” α-actinins) are present in practically every tissue. α-Actinin 4 has a molecular weight of ~100 kDa and functions as an antiparallel homodimer, enabling the N-terminal lateral domains to bundle actin filaments. α-Actinin 4 is ubiquitously expressed in normal non-muscle cells and has been reported in neoplastic tissue with varying levels. Spectrin-related proteins share a similar domain architecture: (1) an N-terminal actin-binding site formed by a pair of calponin-homology (CH) domains; (2) a central rod domain consisting of spectrin-like repeats that can serve as docking sites for cytosolic and nuclear proteins; (3) a C-terminal calmodulin-like domain with two EF-hand motifs. α-Actinin 4 predominantly localizes in the cytoplasm and has also been detected in the nucleus in some cells. Activation of intracellular pathways or actin filament depolymerization may trigger nuclear translocation. |
| Actin interaction | Actin cross-linking protein. Kd (actin-binding) = 1–5 µM. |
Properties
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2 × 50 µg |
| Buffer | 100 mM NaCl, 20 mM Tris-Cl pH 7.4, 0.5 mM DTT and 3% disaccharides, when reconstituted with 50 µl ultrapure water to obtain a 1 mg/ml solution. |
| Purity | >98% by scanning densitometry from Coomassie G-250 stained SDS gels. |
| Purification notes | |
| Protein concentration | Determined by UV-VIS (A280 = 0.1201). |
| Storage instructions | Upon reconstitution store on ice. Can also be stored as a glycerol stock at -20°C. Avoid repeated freeze/thaw cycles. |
| Shipping conditions | At ambient temperature. Upon delivery store at -70°C. |
| Remarks | For research use only. Not for use in human or veterinary diagnostic or therapeutic applications. |
| CAS no. | |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Further Information
Product DataSheet
Material and Safety Data Sheet
Protein Sequence on NCBI
References
Real-time dynamics of emerging actin networks in cell-mimicking compartments.
Deshpande S, Pfohl T. PLoS One. 2015 Mar 18;10(3):e0116521. doi: 10.1371/journal.pone.0116521.
A high molecular mass protein isolated from chicken gizzard: its localization at the dense plaques and dense bodies of smooth muscle and the Z-disks of skeletal muscle.
Terasaki AG, Nakagawa H, Kotani E, Mori H, Ohashi K. J Cell Sci. 1995 Mar;108 (Pt 3):857-68.
