Analytical Data
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Gene name
DIAPH1
- Application
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Alternative Names
DFNA1; DRF1; LFHL1; hDIA1; Diaphanous-related formin-1
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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
O60610
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Expression Region
Asp389~Pro577
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Molecular Weight
26kDa
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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
Diaphanous homolog 1 (DIAPH1) is a key member of the formin family of proteins, which are essential regulators of actin dynamics in various cellular processes, including cell migration, division, and morphogenesis. DIAPH1 has gained significant attention in recent years due to its critical role in cytoskeletal restructuring, influencing not only cellular architecture but also intercellular signaling pathways. Mutations in the DIAPH1 gene have been implicated in several human diseases, such as deafness, and are also associated with certain types of cancer, highlighting its potential as a therapeutic target. Research on DIAPH1 recombinant proteins aims to elucidate its structural and functional characteristics, providing insights into its mechanisms of action. By producing and purifying DIAPH1 in recombinant systems, scientists can study its interaction with actin filaments and assess the effects of specific mutations or post-translational modifications. Furthermore, the use of DIAPH1 recombinant protein in biochemical assays allows for a better understanding of its role in cellular processes and its contribution to pathophysiological conditions. Overall, the study of DIAPH1 recombinant proteins is vital for unraveling the complexities of actin regulation and its implications for health and disease.
