Analytical Data
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Gene name
DCAF11-DDB1
- Application
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Alternative Names
WDR23
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Species
Human
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Source
Baculovirus
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TEB1-1 (G2-Q546)&Q16531-1
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Expression Region
Q8TEB1-1 (G2-Q546)&Q16531-1 (M1-H1140)
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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
DCAF11-DDB1 is a crucial component of the DDB1-CUL4-ROC1 E3 ubiquitin ligase complex, playing a significant role in cellular processes such as DNA damage response, protein degradation, and cell cycle regulation. The DDB1 protein functions as a substrate receptor, recruiting various DCAF (DDB1-CUL4-associated factors) proteins to mediate the ubiquitination of target proteins. Research into DCAF11-DDB1 has garnered attention due to its involvement in the cellular response to DNA lesions, making it particularly relevant in the study of cancer and genetic disorders related to DNA repair defects. Understanding the molecular mechanisms underpinning DCAF11-DDB1 interactions and functions could provide insights into cancer development and highlight potential therapeutic targets for enhancing the efficacy of DNA-damaging agents used in cancer treatment. Furthermore, aberrations in the regulation of DCAF11 have been associated with various pathologies, suggesting its potential as a biomarker for disease progression. Advances in structural biology techniques have enabled researchers to elucidate the three-dimensional structures of DCAF11-DDB1 complexes, providing a foundation for understanding their functional dynamics. As research continues to explore the broader implications of DCAF11-DDB1 in cellular homeostasis and disease, it has become an increasingly important focus within the fields of molecular biology and oncology, highlighting the potential for novel therapeutic applications.
