Analytical Data
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Gene name
Cofilin-1
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简介
Cofilin-1 protein has pH-sensitive F-actin depolymerizing activity and can bind to F-actin. It cooperates with the subcortical maternal complex (SCMC) to guide the fertilized egg through initial embryonic cell division by regulating actin dynamics. Cofilin-1 Protein, Human (His) is the recombinant human-derived Cofilin-1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
Cofilin-1; 18 kDa phosphoprotein; p18; CFL1; CFL
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23528
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Expression Region
M1-L166
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Protein Length
Full Length
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Molecular Weight
21 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Cofilin-1 is a key actin-binding protein that plays a crucial role in regulating cytoskeletal dynamics and maintaining cellular morphology. It is known to bind to actin filaments, promoting their depolymerization and facilitating actin turnover, which is essential for various cellular processes such as cell motility, division, and signaling. Dysregulation of cofilin-1 activity has been implicated in several diseases, including cancer metastasis, neurodegenerative disorders, and cardiac dysfunction. The study of recombinant cofilin-1 protein allows researchers to investigate its structural properties, binding affinities, and functional roles in cellular contexts. By producing purified forms of cofilin-1 through recombinant DNA technology, scientists can perform in-depth analyses of its interactions with actin and other cellular components, as well as examine how post-translational modifications influence its activity. Understanding the molecular mechanisms governing cofilin-1 function is vital for developing targeted therapeutic strategies to mitigate the pathological effects associated with its dysfunction. Thus, the study of cofilin-1 through recombinant protein expression and characterization holds significant promise for advancing our knowledge of cellular dynamics and developing innovative approaches for disease intervention.
