Analytical Data
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Gene name
CFL2
- Application
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Alternative Names
CFL2；Cofilin-2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y281
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Expression Region
1-166aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMASGVTVNDEVIKVFNDMKVRKSSTQEEIK KRKKAVLFCLSDDKRQIIVEEAKQILVGDIGDTVEDPYTSFVKLLPLNDC RYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTG IKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL
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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
CFL2 (Cofilin-2) is an actin-binding protein primarily expressed in skeletal muscle and has garnered significant attention in research due to its crucial role in actin dynamics and cellular functions. Actin filaments, the primary components of the cytoskeleton, are essential for various cellular processes including motility, division, and maintaining cell shape. CFL2 is known to regulate actin polymerization and depolymerization, which directly influences muscle contraction and development. Abnormal expression or mutations in CFL2 have been implicated in various muscle disorders and diseases, highlighting its importance in muscle biology. Additionally, studying CFL2 at the molecular level can offer insights into the fundamental mechanisms of muscle-related pathologies and may inform therapeutic strategies. Researchers have focused on the recombinant expression of CFL2 to better understand its structure-function relationship, interactions with other proteins, and its regulatory mechanisms. The recombinant proteins can serve as valuable tools in functional assays to elucidate CFL2’s roles in the actin cytoskeleton and its potential involvement in diseases, making it a significant subject in current biomedical research.
