Tropomyosin (cardiac Tropomyosin) - 2x100µg
Tropomyosin
From cardiac muscle, porcine.
Description
| Protein | Tropomyosin |
| Origin | Cardiac muscle, porcine |
| Molecular mass | Approximately 70 kDa |
| Molecular structure | Tropomyosin is an elongated, coiled-coil protein that assembles as a parallel dimer of α-helical chains. Cardiac muscle tropomyosin contains α- and β-tropomyosin chains and forms a rod-like molecule that binds along the major groove of F-actin. Each tropomyosin molecule spans approximately seven actin subunits on the filament and contributes to the cooperative regulation of actin filament dynamics and actomyosin interaction. |
| Actin interaction | Binds laterally to F-actin at a molar ratio of 1:7 tropomyosin:G-actin. |
Properties
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2 × 100 µg |
| Buffer | 0.05 M KCl, 20 mM imidazole pH 7.4, 1 mM EDTA, 1 mM DTT and 2.5% disaccharides, when reconstituted with ultrapure water to obtain a 1 mg/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, store the product on ice. The 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 research use only. Not for use in human or veterinary diagnostic or therapeutic applications. |
| CAS no. | |
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 (all sequences)
Protein Structure on NCBI
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.
Construction of an atomic model for tropomyosin and implications for interactions with actin.
Phillips Jr GN.
J Mol Biol. 1986;192:128.
