Analytical Data
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Gene name
DCAF4
- Application
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Alternative Names
WD repeat-containing protein 21A
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WV16
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Expression Region
1-495aa
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Molecular Weight
71.7 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
DCAF4 (DDB1/CUL4-associated factor 4) is a crucial component of the CUL4-DDB1 E3 ubiquitin ligase complex, which plays an essential role in regulating various cellular processes, including cell cycle progression, DNA repair, and the response to oxidative stress. The function of DCAF4 is primarily mediated through its interaction with specific substrate proteins, facilitating their ubiquitination and subsequent proteasomal degradation. Recent studies have highlighted the significance of DCAF4 in maintaining cellular homeostasis and its potential implications in oncogenesis, as aberrations in the ubiquitination process are often linked to cancer development. Furthermore, DCAF4 has been identified as a critical regulator of the cellular response to DNA damage, contributing to the repair mechanisms that preserve genomic integrity. Understanding the structural and functional dynamics of DCAF4, particularly through the analysis of its recombinant protein, could unveil new therapeutic avenues for targeting diseases driven by dysregulated protein homeostasis. This research background emphasizes the necessity of exploring DCAF4's molecular mechanisms and its role in broader biological contexts, making it a compelling target for further investigation in cancer biology and therapeutic development.
