Analytical Data
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Gene name
DAP6
- Application
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Alternative Names
DAXX; BING2; EAP1; ETS1-associated protein 1; Fas death domain-associated protein
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UER7
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Expression Region
Met1~Pro160
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Molecular Weight
51kDa
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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
DAP6, or Death Associated Protein 6, is a crucial protein involved in various cellular processes, particularly in the regulation of apoptosis and immune responses. Initially identified for its role in cell death mechanisms, DAP6 has garnered attention due to its influence on immune system functions, including T cell activation and cytokine production. Research on DAP6 has expanded to explore its potential as a biomarker for various diseases, especially in cancer and autoimmune disorders. The protein's involvement in signaling pathways sheds light on its significance in both normal physiological processes and pathological conditions. Furthermore, investigating DAP6 as a recombinant protein enables detailed studies of its structural characteristics and interactions with other cellular molecules, facilitating the understanding of its molecular mechanisms. The study of DAP6 could lead to innovative therapeutic strategies targeting immune regulation and apoptosis, highlighting its potential in medical research and drug development. Given the growing interest, the characterization and functional analysis of DAP6 as a recombinant protein holds promise for advancements in understanding various diseases and developing novel treatments.
