Gelsolin (plasma, bovine)
(Actin Binding Protein)
Cat. #: 8315-01
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Description
|
Protein |
Gelsolin (plasma isoform) |
|
Origin |
Plasma, bovine |
|
Molecular mass |
83kDa |
|
Protein description |
Plasma gelsolin has a molecular mass of 83kDa and consists of six homologous subdomains (S1-S6). Gelsolin is a Ca++-dependent lipid binding actin regulatory protein, possessing three different actin modulating activities: severing of F-actin, nucleation of actin polymerization and capping of filaments barbed end. Gelsolin has three actin binding sites, two high affinity Ca++ binding sites and two binding sites for PIP2. |
|
Actin interaction |
Ca++-sensitive actin capping, nucleating and severing protein. Kd actin-binding = 50nM (barbed end). |
Properties
|
Form |
Lyophilized, ready-to-use. |
|
Quantity |
2x50 µg |
|
Buffer |
10mM Imidazole pH 7.0, 0.2mM DTT, 0.2mM EGTA, 2mM NaN3 and 1% disaccharides, when reconstituted with 50 µl ultrapure water to obtain a 1.0 mg/ml solution. |
|
Purity & Activity |
Purity: >93% by scanning densitometry from Coomassie G-250 stained SDS-Gels. Fragmentation activity: The fragmentation activity of gelsolin was determined by Ostwald viscometry at 25°C. The specific viscosity of F-actin (1mg/ml) is reduced by ~65% after addition of gelsolin at a molar ratio of 1:100. The gelsolin stock solution was used as described below containing 1% disaccharides. F-actin containing 100mM KCl, 10mM Imidazole pH 7.4, 1mM ATP was mixed with 0.2mM CaCl2 (final concentration) prior to the addition of gelsolin. |
|
Purification notes |
Purified from bovine plasma. GPC, IEXC. |
|
Protein concentration |
Determined by Biuret method with actin (skeletal muscle, rabbit) as reference. |
|
Storage instructions |
Gelsolin 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 decrease of the activity, and has to be 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 NCBI *Protein Structure on NCBI (PDB ID: 1D0N - gelsolin from equus caballus)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
PI3Kα-regulated gelsolin activity is a critical determinant of cardiac cytoskeletal remodeling and heart disease.
Patel VB, Zhabyeyev P, Chen X, Wang F, Paul M, Fan D, McLean BA, Basu R, Zhang P, Shah S, Dawson JF, Pyle WG, Hazra M, Kassiri Z, Hazra S, Vanhaesebroeck B, McCulloch CA, Oudit GY. Nat Commun. 2018 Dec 19;9(1):5390. doi: 10.1038/s41467-018-07812-8.
A myosin II nanomachine mimicking the striated muscle..
Pertici I, Bongini L, Melli L, Bianchi G, Salvi L, Falorsi G, Squarci C, Bozó T, Cojoc D, Kellermayer MSZ, Lombardi V, Bianco P.; Nat Commun. 2018 Aug 30;9(1):3532.
Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats.
Way M, Weeds A.; J Mol Biol. 1988 Oct 20;203(4):1127-33.
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 DataSheetMaterial and Safety Data SheetProtein Sequence on NCBI *Protein Structure on NCBI (PDB ID: 1D0N - gelsolin from equus caballus)
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
PI3Kα-regulated gelsolin activity is a critical determinant of cardiac cytoskeletal remodeling and heart disease.
Patel VB, Zhabyeyev P, Chen X, Wang F, Paul M, Fan D, McLean BA, Basu R, Zhang P, Shah S, Dawson JF, Pyle WG, Hazra M, Kassiri Z, Hazra S, Vanhaesebroeck B, McCulloch CA, Oudit GY. Nat Commun. 2018 Dec 19;9(1):5390. doi: 10.1038/s41467-018-07812-8.
A myosin II nanomachine mimicking the striated muscle..
Pertici I, Bongini L, Melli L, Bianchi G, Salvi L, Falorsi G, Squarci C, Bozó T, Cojoc D, Kellermayer MSZ, Lombardi V, Bianco P.; Nat Commun. 2018 Aug 30;9(1):3532.
Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats.
Way M, Weeds A.; J Mol Biol. 1988 Oct 20;203(4):1127-33.
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.
