Analytical Data
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Gene name
TWF1
- Application
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Alternative Names
TWF1；PTK9；Twinfilin-1
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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
Q12792
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Expression Region
100-350aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHM MLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD
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Molecular Weight
32 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
TWF1, or twinfilin 1, is a key actin-binding protein that plays a crucial role in the regulation of the cytoskeleton, which is fundamental for various cellular processes, including cell motility, shape, and division. Research into TWF1 has gained traction due to its involvement in several physiological and pathological conditions, such as cancer metastasis and neurodegenerative diseases. The protein is known to bind to actin filaments, preventing their disassembly and thereby stabilizing the cytoskeletal network. Recent studies have focused on the structural and functional characterization of TWF1, which could lead to a better understanding of its regulatory mechanisms and interactions with other cellular components. Furthermore, TWF1's potential as a therapeutic target is being explored, particularly in relation to its role in tumor progression and the maintenance of neuronal integrity. The generation of recombinant TWF1 protein is critical for these investigations, enabling researchers to conduct various biochemical assays, structural analyses, and functional studies. By delineating the precise roles of TWF1 in cellular dynamics, scientists aim to uncover novel insights into its contributions to health and disease, paving the way for innovative therapeutic strategies.
