Analytical Data
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Gene name
DIAPH1
- Application
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Alternative Names
DIAPH1；DIAP1；Protein diaphanous homolog 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
O60610
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Expression Region
全长
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AA Sequence
full
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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
Related Products
Protein Description
DIAPH1 (Diaphanous-related formin 1) is a mammalian homolog of the Drosophila diaphanous protein, which plays a crucial role in actin dynamics and cytoskeletal organization. As a member of the formin family, DIAPH1 is known for its ability to promote the nucleation and elongation of actin filaments, thus influencing various cellular processes, including cell shape, motility, and division. Dysregulation of DIAPH1 has been implicated in several diseases, including developmental disorders and cancer, where altered cell migration and invasion are observed. The study of DIAPH1 has gained significant attention due to its potential as a therapeutic target. Researchers are particularly interested in its reorganization during cytokinesis and its interactions with other cytoskeletal proteins. Understanding the structural and functional properties of DIAPH1 through recombinant protein studies can provide insights into its mechanism of action and its role in health and disease. Recombinant DIAPH1 proteins offer a valuable tool for elucidating these functions in vitro, enabling detailed investigations into its biophysical properties, expression patterns, and interactions with various cellular components. This research ultimately aims to develop novel therapeutic strategies that could manipulate DIAPH1 activity for potential clinical applications.
