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Actin Binding Protein, Cofilin
The twisted clue to depolymerize actin.
Cofilin
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The ubiquitous actin-binding protein protein
reorganizes the actin cytoskeletons. Members of
the ADF/Cofilin family bind to actin monomers and
depolymerize actin filaments 1. by severing and 2.
by increasing the off-rate for actin monomers from
the pointed end. cofilin changes structure of the actin
filaments and makes it twisted to facilitate interaction.
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Actin Binding Protein
Description
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Protein
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Cofilin (synonym: n-cofilin , cofilin-1)
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Origin
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non-muscle isoform, murine recombinant (untagged)
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Molecular mass
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18.5kDa
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Protein description
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Cofilin depolymerizes actin filaments and inhibits polymerization of G-actin in a
pH-sensitive manner. it is a regulatory protein of cytoskeletal actin dynamics.
Cofilin plays a role in the regulation of cell morphology and cytoskeletal organization.
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Actin interaction
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Non-muscle cofilin binds to G- and F-actin in a 1:1 molar ratio.
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Properties
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Form
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Lyophilized, ready-to-use
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Quantity
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50 µg
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Buffer
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150mM NaCl, 20mM Hepes pH 7.4, 1mM DTT and 5% sucrose, when reconstituted
with 1.0ml ultrapure water to obtain a 1.0 mg/ml solution.
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Purity
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>96% by scanning densitometry from Coomassie G-250 stained SDS-Gels.
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Purification notes
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Cofilin was expressed as a GST-tag fusion protein in E. coli. After purification by
GST-Agarose and subsequent GST-tag cleavage, the pure protein was yielded by
gel filtration chromatography.
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Protein conc.
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Determined by OD280 (0.1%=0.778).
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Storage instructions
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Cofilin 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 stored at -20°C. in glycerol or cryoprotect (Cat.#: 6011-01).
Avoid repeated freeze / thaw cycles.
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Shipping conditions
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At ambient temperature. Upon delivery store at -70°C.
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Remarks
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For Use in Research only. Not for Use in Human or Veterinary Diagnostical or
Therapeutical Applications.
|
Actin Binding Protein
Description
|
Protein
|
|
Cofilin (synonym: n-cofilin , cofilin-1)
|
|
Origin
|
|
non-muscle isoform, murine recombinant (untagged)
|
|
Molecular mass
|
|
18.5kDa
|
|
Protein description
|
|
Cofilin depolymerizes actin filaments and inhibits polymerization of G-actin in a
pH-sensitive manner. it is a regulatory protein of cytoskeletal actin dynamics.
Cofilin plays a role in the regulation of cell morphology and cytoskeletal organization.
|
|
Actin interaction
|
|
Non-muscle cofilin binds to G- and F-actin in a 1:1 molar ratio.
|
Properties
|
Form
|
|
Lyophilized, ready-to-use
|
|
Quantity
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1.0mg
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|
Buffer
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|
150mM NaCl, 20mM Hepes pH 7.4, 1mM DTT and 5% sucrose, when reconstituted
with 1.0ml ultrapure water to obtain a 1.0 mg/ml solution.
|
|
Purity
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>96% by scanning densitometry from Coomassie G-250 stained SDS-Gels.
|
|
Purification notes
|
|
Cofilin was expressed as a GST-tag fusion protein in E. coli. After purification by
GST-Agarose and subsequent GST-tag cleavage, the pure protein was yielded by
gel filtration chromatography.
.
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|
Protein conc.
|
|
Determined by OD280 (0.1%=0.778).
|
|
Storage instructions
|
|
Cofilin 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 stored at -20°C. in glycerol or cryoprotect (Cat.#: 6011-01).
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.
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