Actin
alpha-actin from skeletal muscle, rabbit
| Protein | Actin (α-Actin) |
| Origin | Skeletal muscle alpha actin, rabbit |
| Molecular mass | 42 kDa |
| Protein description | Actin from rabbit skeletal muscle is a single-chain polypeptide with a molecular weight of 42 kDa consisting of 375 amino acids. It binds ATP/ADP and contains binding sites for divalent cations that contribute to actin stabilization. Actin is a multi-ligand protein and a major component of the cytoskeleton. The skeletal muscle actin (alpha-actin isoform) is highly conserved among vertebrates, which is why rabbit skeletal muscle actin is frequently used to investigate protein–protein interactions with cytoskeletal ligands. Actin monomer integrity and polymerization competence (filament formation, higher-order assemblies, and characteristic kinetics) depend strongly on actin quality and assay conditions (e.g., nucleotide state, divalent cations, ionic strength). Hypermol provides premium-quality actin conserved by a proprietary freeze-drying approach to support high functional activity after reconstitution. |
| Purity | >99% by scanning densitometry. |
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2 × 500 µg |
| Buffer | 2 mM Tris-Cl pH 8.2, 0.4 mM ATP, 0.5 mM DTT, 0.1 mM CaCl2, 1 mM NaN3 and 0.3% disaccharides, when reconstituted with 1.0 ml ultrapure water to obtain a 1 mg/ml solution. |
| Related products | For dilution of G-actin or exchange of ligand buffer into actin compatible buffer, MonoMix (Cat. #: 5100-0*) may be used. In the absence of nucleators, polymerization of G-actin is initiated by PolyMix (Cat. #: 5000-0*). |
| Purification notes | Purified from rabbit skeletal muscle, GPC. |
| Protein concentration | Determined by the Biuret method. |
| Storage instructions | Actin stored at −70 °C upon arrival will be stable in performance for at least 6 months from the date of purchase. Solubilized G-actin is kept on ice and should be used within 1 week. Avoid refreezing. |
| 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. | 51005-14-2 |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
Cosolvent and crowding effects on the polymerization kinetics of actin.
Rosin, Christopher, Paul Hendrik Schummel and Robert S. C. Winter.
Physical Chemistry Chemical Physics: PCCP 17(13) (2015): 8330–8337.
Exploring the stability limits of actin and its suprastructures.
Rosin C, Erlkamp M, Ecken JV, Raunser S, Winter R.
Biophys J. 2014 Dec 16;107(12):2982–2992. doi: 10.1016/j.bpj.2014.11.006.
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.
Cabrales Fontela Y, Kadavath H, Biernat J, Riedel D, Mandelkow E, Zweckstetter M.
Nat Commun. 2017 Dec 7;8(1):1981. doi: 10.1038/s41467-017-02230-8.
