Vinculin tail(Actin Binding Protein)Cat. #: 8327-01.............................................................................................................................................................................................................................................................................................................................................................................................................
Description
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Protein | Vinculin tail |
Origin | Smooth muscle, turkey |
Molecular mass | 29/27kDa |
Protein description | Vinculin tail is obtained by limited cleavage with protease V8 from S. aureus of natively prepared smooth muscle vinculin from turkey gizzard. The C-terminal tail region (851-1066) binds to F-actin and was shown to bundle actin filaments in vitro (Hüttelmaier et al., 1997).Since vinculin is autoinhibited by a head/tail interaction, the tail region is used to characterize the actin interactions of vinculin. |
Actin interaction | F-Actin binding protein fragment. |
Properties
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Form | Lyophilized, ready-to-use. |
Quantityper unit | 1x50 µg |
Buffer | PBS, 0.5% disaccharides, when reconstituted with 50µlultrapure water to obtain a 1mg/ml solution. |
Purity | >99%by scanning densitometryfrom Coomassie G-250 stained SDS-Gels. |
Purification notes | Purified from turkey gizzard muscle. |
Protein concentration | Determinedby Biuret method. |
Storage instructions | Vinculin tail 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
Characterization of two F-actin-binding and oligomerization sites in the cell-contact proteinvinculin.
Hüttelmaier S, Bubeck P, Rüdiger M,JockuschBM., Eur J Biochem. 1997 Aug 1;247(3):1136-42.
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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