Native Bovine gelsolin is a calcium and polyphosphoinositide regulated actin-binding protein which consists of 6 homologous domains. It is involved in cell morphology, motility, growth and apoptosis. Gelsolin affects filament assembly by severing actin filaments, forming a nucleus for polymerisation, and capping the fast exchanging end of the filaments.
- Target Species
- Product Form
- Purified protein from bovine plasma - lyophilised
- Use sterile distilled water to give a concentrated stock solution => 1 mg/ml.
- Buffer Solution
- Tris buffered saline, EGTA
- Preservative Stabilisers
- See Buffer solution.
- 54 U/mg protein.One unit will reduce the viscosity difference between an actin solution and buffer by 50% in a 1 ml reaction mixture containing 1-2 mg F-actin, 0.15 M KCl, 20 mM TRIS, pH 7.6, 0.2 mM CaCl2, 0.2 mM ATP and 1 mM DTT at 28ºC.
- SDS PAGE: >95%
- Approx. Protein Concentrations
- 5%, remainder buffer salts.
- Prior to reconstitution store at +4oC.
After reconstitution store at -20oC.
Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein.
- Shelf Life
- 12 months from date of despatch.
- Q3SX14 Related reagents
- Entrez Gene
- GSN Related reagents
- GO Terms
- GO:0003779 actin binding
- GO:0005856 cytoskeleton
- GO:0051693 actin filament capping
- For research purposes only
Applications of Gelsolin
|Application Name||Verified||Min Dilution||Max Dilution|
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using the appropriate negative/positive controls.
Copyright © 2018 Bio-Rad Antibodies (formerly AbD Serotec)
Product Specific References
References for Gelsolin
Yin, H. L. & Stossel, T. P. (1980) Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages.
J. Biol. Chem. 255: 9490-9493.
Yin, H. L. et al. (1988) Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments.
J. Cell Biol. 106(3): 805-812.
Sun, H. Q., et al. (1994) The actin side-binding domain of gelsolin also caps actin filaments. Implications for actin filament severing.
J. Biol. Chem. 269(13): 9473-9479.
Burtnick, L. D., et al. (1997) The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.
Cell 90(4): 661-670.