Actin (bovine alpha cardiac actin) - 2x0.5mg
Actin
α-cardiac actin, bovine
Description
| Protein | Actin (α-Actin) |
| Origin | Cardiac muscle alpha actin, bovine |
| Molecular mass | 42 kDa |
| Protein description | Actin from bovine cardiac muscle is a single chain polypeptide with a molecular weight of 42 kDa consisting of 375 amino acids. |
| Purity | >99% by scanning densitometry. |
Properties
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2x 0.5 mg |
| 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, the polymerization of G-actin is initiated by PolyMix (Cat. #: 5000-0*). |
| Purification notes | Purified from bovine cardiac 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 |
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
Lymphocyte-specific protein 1 regulates mechanosensory oscillation of podosomes and actin isoform-based actomyosin symmetry breaking.
Cervero P, Wiesner C, Bouissou A, Poincloux R, Linder S.
Nat Commun. 2018 Feb 6;9(1):515. doi: 10.1038/s41467-018-02904-x.
Cervero P, Wiesner C, Bouissou A, Poincloux R, Linder S.
Nat Commun. 2018 Feb 6;9(1):515. doi: 10.1038/s41467-018-02904-x.
