Analytical Data
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Gene name
DRAP1
- Application
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Alternative Names
Dr1-associated protein 1Negative cofactor 2-alpha ;NC2-alpha
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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
Q14919
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Expression Region
4-198aa
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Molecular Weight
48.2 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
DRAP1 (DRAP1, also known as D1 protein) is a critical regulator of the cellular response to various stressors and is implicated in several essential biological processes, such as apoptosis and cell proliferation. Research into DRAP1 has gained momentum due to its potential role in the pathophysiology of various diseases, including cancers and neurodegenerative disorders. The protein interacts with several key signaling pathways, particularly those involving the tumor suppressor p53 and the apoptosis regulator Bcl-2, suggesting that it may play a pivotal role in maintaining cellular homeostasis under stress conditions. Recent studies have focused on the development and characterization of recombinant DRAP1 protein to better understand its structure-function relationships and biological activities. Recombinant protein production allows for the investigation of DRAP1’s conformational states, oligomerization, and interaction with other proteins, which is crucial for elucidating its functional mechanisms. Additionally, the use of recombinant DRAP1 in experimental settings is paving the way for potential therapeutic applications, as modulating its activity could yield novel strategies for cancer treatment and neuroprotection. Continued research on DRAP1 and its recombinant forms is necessary to establish its role as a biomarker for disease progression and to explore its therapeutic potential in the modulation of apoptotic pathways.
