Tropomyosin (cardiac Tropomyosin) - 2x100µg
Tropomyosin
(from cardiac muscle)
Cat. #: 8308-01
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Description
Protein |
Tropomyosin |
Origin |
cardiac muscle, porcine |
Molecular mass |
~70kDa |
Molecular structure |
Heterodimeric protein (α,β), consisting of alpha helical coiled coils, that binds laterally to the actin filament in muscle and non-muscle cells. |
Actin interaction |
Laterally binds to F-actin at a molar ratio of 1:7 (tropomyosin:g-actin). |
Properties
Form |
Lyophilized, ready-to-use. |
Quantity per unit |
2x100 µg |
Buffer |
0.05M KCl, 20mM imidazole pH 7.4, 1mM EDTA, 1mM DTT and 2.5% disaccharides, when reconstituted with ultrapure water to obtain a 1mg/ml solution. |
Purity |
>98% by scanning densitometry. |
Purification notes |
Purified from porcine cardiac muscle. |
Protein concentration |
Determined by the Biuret method. |
Storage instructions |
Upon reconstitution the product is stored on ice. This product 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 Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
CAS no. |
Further Information
References
Cooperative effects of tropomyosin on the dynamics of the actin filament.
Khaitlina S, Tsaplina O, Hinssen H.
FEBS Lett. 2017 Jul;591(13):1884-1891. doi: 10.1002/1873-3468.12700. Epub 2017 Jun 11.
Cooperative effects of tropomyosin on the dynamics of the actin filament.
Khaitlina S, Tsaplina O, Hinssen H.
FEBS Lett. 2017 Jul;591(13):1884-1891. doi: 10.1002/1873-3468.12700. Epub 2017 Jun 11.
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