Analytical Data
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Gene name
DDI1
- Application
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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
Q8WTU0
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Expression Region
Met1~His396
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Molecular Weight
48kDa
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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
DDI1 (DNA damage-inducible 1) is a protein that plays a crucial role in cellular stress response, particularly in the context of DNA damage and proteostasis. The study of DDI1 has gained importance due to its involvement in various cellular processes, including the regulation of protein degradation pathways and the maintenance of genomic stability. Research indicates that DDI1 is upregulated in response to DNA damage, suggesting that it may act as a protective factor against genotoxic stress. This protein is also linked to the ubiquitin-proteasome system, a key pathway for protein turnover that is essential for cellular function and response to environmental stressors. Investigating recombinant DDI1 protein offers insights into its structure and function, which could lead to the development of potential therapeutic approaches for diseases characterized by DNA repair deficiencies, such as cancer. Furthermore, understanding DDI1's mechanism may provide valuable information for enhancing the efficacy of therapies that target tumor cells by exploiting their reliance on stress response pathways. As a result, the study of DDI1 not only contributes to the fundamental knowledge of cellular responses to damage but also holds promise for novel therapeutic strategies in cancer treatment and other related diseases. Researchers are focused on characterizing DDI1's interactions and its role in signaling pathways, which is crucial for unraveling its potential as a biomarker or target in clinical settings.
