Actin
alpha-actin from skeletal muscle, rabbit
| Protein | Actin (α-Actin) |
| Origin | Skeletal muscle, 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 (ATPase function) 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. The ability of actin monomers to polymerize into filaments, to form higher-order assemblies, and to show typical actin kinetics depends strongly on actin quality and on assay conditions (e.g., nucleotide state, divalent cations, ionic strength). Hypermol actin is provided as a premium-quality preparation 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 | 4 × 250 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 0.25 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 Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
| CAS no. | 51005-14-2 |
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.
Product DataSheetMaterial and Safety Data SheetProtein Sequence on NCBI
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): 8330-7.
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.
