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Vinculin (smooth muscle, turkey) - 100 µg

Cat. #:
8307-01
Shipping:
FedEx Express (Global) FedEx Express (Global) (shipping info)
Quantity:
100 µg
Units:
1x
5x ( + 668,00 EUR )



Vinculin
(Actin Binding Protein)


Cat. #: 8307-01

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Description

   

Protein

Vinculin

Origin

Smooth muscle, turkey

Molecular mass

116kDa

Protein description

Vinculin from turkey smooth muscle (gizzard) is a single chain polypeptide with a molecular weight of 116kD. Vinculin is a multiligand binding protein e.g. of focal contacts, possessing an F-actin binding domain in the tail region.

Vinculin is supplied in the native inactive state, characterized by the interaction of the vinculin head and tail, which can be released e.g. by phospholipids.

Actin interaction

Actin binding protein. 




Properties

   

Form

Lyophilized, ready-to-use.

Quantity per unit

1x100 µg

Buffer

100mM KCl, 10mM imidazole pH 7.5, 0.5mM DTT, 0.1mM EGTA and 0.25% disaccharides, when reconstituted with 100 µl ultrapure water to obtain a 1.0 mg/ml solution.

Purity

>98% by scanning densitometry from Coomassie G-250 stained SDS-Gels.

Purification notes

Purified from turkey gizzard muscle.

Protein concentration

Determined by Biuret method.

Storage instructions

Vinculin is stored at –70°C upon arrival and will be stable in performance for at least 6 months from the date of purchase. The solubilized protein is kept on ice and should be used within 2-3 weeks. 

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

Protein Sequence on NCBI

Protein Sequences and Structures on RCSB

Material and Safety Data Sheet

 



References  
 
Binding of Vinculin to Lipid Membranes in Its Inhibited and Activated States.
Dwivedi M, Winter R.
Biophys J. 2016 Oct 4;111(7):1444-1453. doi: 10.1016/j.bpj.2016.08.019.

 

Structural basis for vinculin activation at sites of cell adhesion.
Bakolitsa C, Cohen DM, Bankston LA, Bobkov AA, Cadwell GW, Jennings L, Critchley DR, Craig SW, Liddington RC. 
Nature. 2004 Jul 29;430(6999):583-6. Epub 2004 Jun 13.


 
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