Tropomyosin/Troponin
(Actin Binding Protein)
Cat. #: 8321-01
.............................................................................................................................................................................................................................................................................................................................................................................................................
Description
|
|
Protein
|
Tropomyosin-Troponin (Synonym: native Tropomyosin)
|
Origin
|
Skeletal muscle, rabbit
|
Molecular mass
|
~148kDa
|
Molecular structure
|
Tropomyosin (2x35kDa), Troponin T (37kDa),Troponin I (23kDa),Troponin C (18kDa).
|
Actin interaction
|
Ca++-sensitive, regulatory laterally F-actin binding complex. Molar ratio = 1:7 (tropomyosin/troponin:g-actin).
|
Properties
|
|
Form
|
Lyophilized, ready-to-use.
|
Quantity per unit
|
2x100 µg
|
Buffer
|
0.1M KCl, 20mM imidazole pH 7.4, 1mM EDTA, 2mM DTT and 2% disaccharides, when reconstituted with 100µl ultrapure water to obtain a 1mg/ml solution.
|
Purity
|
>95% by scanning densitometry.
|
Purification notes
|
Purified from rabbit skeletal muscle.
|
Protein concentration
|
Determined by the Biuret method.
|
Storage instructions
|
Tropomyosin/Troponin is stored at –70°C upon arrival will be stable in performance for at least 6 months from the date of purchase. The solubilized complex is kept on ice and should be used within 1 week.
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
Product DataSheet
Material and Safety Data Sheet
Protein Sequences and Structures on RCSB
The PDB link contains the sequences of troponins, tropomyosin and actin from skeletal muscle (rabbit and chicken) and were given in the publication cited below.
References
Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA
Plos One (2010) 5 p.126433