Gelsolin GLN40 (TL40)
(N-terminal cytoplasmic gelsolin - mouse recombinant)
(Actin Binding Protein)
Cat. #: 8325-01
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Applications
- Fragmentation assays in the absence of Ca++ (permits the presence of EGTA);
- Easy and efficient removal of F-actin from the cellular or myofibrillar cytoskeleton;
Description
|
Protein |
Gelsolin GLN40 - TL40 (N-terminal cytoplasmic gelsolin) |
|
Origin |
mouse, recombinant |
|
Molecular mass |
40kDa |
|
Protein description |
Recombinant mouse GLN40 (synonym: TL40) is the N-terminal part of mouse gelsolin and comprises the homologous gelsolin subdomains S1-S3 (aa 1-361, molacular mass: ~40kD). |
|
Actin interaction |
Ca++-insensitive F-actin severing. |
Properties
|
Form |
Lyophilized, ready-to-use. |
|
Quantity |
1x50 µg |
|
Buffer |
Lyophilized TL40 (50µg) contains 20mM imidazole pH 7.2, 50mM KCl, 1.0mM EGTA and 0.1mM DTT and 0.5% disaccharides, when reconstituted with 50µl ultrapure water to obtain a 1.0 mg/ml solution. |
|
Purity & Activity |
Purity: >98% by scanning densitometry from Coomassie G-250 stained SDS-Gels.
Fragmentation activity: The fragmentation activity of TL40 was determined by Ostwald viscometry at 25°C. The specific viscosity of F-actin (1mg/ml) is reduced by <42% after addition of TL40 at a molar ratio of 1 : 50 (TL40 : A) within less than 2min. |
|
Purification notes |
GPC, IEXC. |
|
Protein concentration |
Determined at A280 0.1209 = 1mg/ml |
|
Storage instructions |
TL40 is stored at –70°C upon arrival 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 5 days. Storage in glycerol at -20°C results in a significant decrase of the activity, and has to determined individually. |
|
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 Sequence on NCBIProtein Structure on NCBI (PDB ID: 1D0N)Please note that the structure PDB ID 1D0N is identical with cytoplasmic gelsolin, since it lacks the N-terminal extension of plasma gelsolin used for crystallization.
References
A Myosin II-Based Nanomachine Devised for the Study of Ca(2+)-Dependent Mechanisms of Muscle Regulation.
Pertici I, Bianchi G, Bongini L, Lombardi V, Bianco P.Int J Mol Sci. 2020 Oct 6;21(19):7372. doi: 10.3390/ijms21197372.PMID: 33036217
Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.
Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13713-8.
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.
Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC.; Cell. 1997 Aug 22;90(4):661-70.
Product DataSheet
Material and Safety Data Sheet
Protein Sequence on NCBIProtein Structure on NCBI (PDB ID: 1D0N)Please note that the structure PDB ID 1D0N is identical with cytoplasmic gelsolin, since it lacks the N-terminal extension of plasma gelsolin used for crystallization.
A Myosin II-Based Nanomachine Devised for the Study of Ca(2+)-Dependent Mechanisms of Muscle Regulation.
Pertici I, Bianchi G, Bongini L, Lombardi V, Bianco P.Int J Mol Sci. 2020 Oct 6;21(19):7372. doi: 10.3390/ijms21197372.PMID: 33036217
Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.
Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13713-8.
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.
Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC.; Cell. 1997 Aug 22;90(4):661-70.
