Analytical Data
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Gene name
TWF1
- Application
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Alternative Names
A6; PTK9; Actin-Binding Protein,Homolog 1; Protein Tyrosine Kinase 9
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q12792
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Expression Region
Met1~Arg184
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Molecular Weight
27kDa
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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
TWF1, or twinfilin 1, is a crucial actin-binding protein implicated in the regulation of cytoskeletal dynamics, particularly in the context of cell motility and morphology. Studies have shown that TWF1 plays a significant role in maintaining cellular architecture by facilitating the disassembly of actin filaments and participating in the recycling of actin monomers. Its dysfunction has been associated with various pathological conditions, including cancer metastasis and neurological disorders, highlighting its importance in both cellular health and disease. The recombinant expression of TWF1 has become a focal point in research, as generating this protein in a laboratory setting allows for detailed characterization of its biochemical properties and interactions with other cellular components. Understanding the precise functioning of TWF1 through recombinant protein studies can lead to insights into its role in cellular processes and may unveil potential therapeutic targets for diseases linked to cytoskeletal dysfunction. The ability to produce TWF1 in sufficient quantities also paves the way for high-throughput screening of small molecules that could modulate its activity, further enhancing our understanding of actin dynamics in cells.
