Analytical Data
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Gene name
DAXX
- Application
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Alternative Names
Daxx ;hDaxxETS1-associated protein 1 ;EAP1Fas death domain-associated protein
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Species
Human
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Source
E. coli
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Tag
N- 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
1-233aa
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Molecular Weight
52.7 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
DAXX (Death Domain-Associated Protein) is a multifunctional protein involved in diverse cellular processes, including apoptosis, transcriptional regulation, and chromatin remodeling. Research into DAXX has gained momentum due to its critical role in various human diseases, particularly cancers and neurodegenerative disorders. DAXX is known to interact with a plethora of signaling proteins, such as the tumor suppressor p53 and histone deacetylases, implicating its involvement in the modulation of gene expression and cell fate decisions. Furthermore, studies have revealed that DAXX can function both as a tumor suppressor and a potential oncogene, depending on the cellular context and mutations present. The complexity of DAXX's interactions and its dual roles have led to increased interest in understanding its structural dynamics, post-translational modifications, and the mechanisms underlying its diverse functions. Recent advancements in techniques such as X-ray crystallography and cryo-electron microscopy have paved the way for detailed analyses of DAXX's structure, providing insights into how its conformation influences its binding to various partners. As ongoing research continues to unravel the precise mechanisms by which DAXX contributes to disease pathology, it holds promise as a potential therapeutic target, making its study crucial in the pursuit of effective treatments for cancer and other associated diseases.
