Analytical Data
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Gene name
DCAF9/DDB1
- Application
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Alternative Names
KIAA1037
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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
Q8N5D0-1 (A2-S677)&Q16531-1
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Expression Region
Q8N5D0-1 (A2-S677)&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
DCAF9 (DDB1 and CUL4-associated factor 9) is a protein that plays a crucial role in various cellular processes, including DNA damage response and protein degradation through the ubiquitin-proteasome pathway. It forms a part of the DDB1-CUL4-RING E3 ubiquitin ligase complex, which mediates the attachment of ubiquitin molecules to target proteins, marking them for degradation. Research on DCAF9 is particularly significant due to its involvement in regulating cellular responses to genotoxic stress and maintaining genomic stability. Aberrant function or expression of DCAF9 has been linked to various diseases, including cancer, highlighting its potential as a therapeutic target. Studies have shown that DCAF9 interacts with specific substrates, influencing cell cycle progression and apoptosis. Understanding the mechanistic aspects of DCAF9/DDB1 interactions can provide insights into their roles in tumorigenesis and stress response pathways. Ongoing research aims to elucidate the structural and functional dynamics of this protein complex in order to develop novel strategies for cancer treatment and enhance our comprehension of the cellular homeostasis mechanisms.
