Analytical Data
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Gene name
DCAF2-DDB1
- Application
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Alternative Names
CDT2; CDW1; DCAF2; L2DTL; RAMP
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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
Q9NZJ0-1 (L2-L730)&Q16531-1
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Expression Region
Q9NZJ0-1 (L2-L730)&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
DCAF2-DDB1 is a pivotal protein complex involved in the regulation of various cellular processes, particularly in the context of DNA damage response and ubiquitin-mediated proteolysis. DCAF2, a substrate receptor of the DDB1-CUL4-RBX1 E3 ubiquitin ligase complex, plays a crucial role in targeting specific proteins for ubiquitination, thereby influencing their stability and function. The study of DCAF2-DDB1 has gained attention due to its implications in cancer biology, where dysregulation of ubiquitination pathways can lead to tumorigenesis. Recent research has unveiled its involvement in the recognition and degradation of cellular factors that regulate cell cycle progression and DNA repair mechanisms. Understanding the molecular mechanisms by which DCAF2-DDB1 operates not only sheds light on fundamental biological processes but also highlights potential therapeutic targets in cancer treatment. As researchers continue to explore the structural and functional aspects of the DCAF2-DDB1 complex, it opens avenues for developing novel strategies to manipulate its activity, with the aim of enhancing the efficacy of cancer therapies or mitigating resistance mechanisms. Moreover, the intricate interplay between DCAF2-DDB1 and other signaling pathways underscores the complexity of cellular homeostasis, making it a vital focus in both basic and applied biomedical research.
