Actin
α-cardiac actin, bovine
Cat. #: 8201-02
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Description
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Protein |
Actin (α-Actin) |
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Origin |
Cardiac muscle alpha actin, bovine |
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Molecular mass |
42kDa |
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Protein description |
Actin from bovine cardiac muscle is a single chain polypeptide with a molecular weight of 42kD consisting of 375 amino acids. |
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Purity |
>99% by scanning densitometry. |
Properties
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Form |
Lyophilized, ready-to-use. |
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Quantity per unit |
1x1 mg |
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Buffer |
2mM Tris-Cl pH 8.2, 0.4mM ATP, 0.5mM DTT, 0.1mM CaCl2, 1mM NaN3 and 0.3% disaccharides, when reconstituted with 1.0 ml ultrapure water to obtain a 1mg/ml solution. |
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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*). |
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Purification notes |
Purified from bovine cardiac muscle, GPC. |
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Protein concentration |
Determined by the Biuret method. |
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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. |
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Shipping conditions |
At ambient temperature. Upon delivery store at -70°C. |
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Remarks |
For Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
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CAS no. |
51005-14-2 |
Further Information
Product DataSheet
Material and Safety Data Sheet
Protein Sequence on NCBI
Lymphocyte-specific protein 1 regulates mechanosensory oscillation of podosomes and actin isoform-based actomyosinsymmetry 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.
Product DataSheetMaterial and Safety Data SheetProtein Sequence on NCBI
Lymphocyte-specific protein 1 regulates mechanosensory oscillation of podosomes and actin isoform-based actomyosinsymmetry 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.
