Analytical Data
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Gene name
DCAF10-DDB1
- Application
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Alternative Names
WDR32
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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
Q5QP82 (F2-F559)&Q16531-1
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Expression Region
Q5QP82 (F2-F559)&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
DCAF10-DDB1 is a crucial protein complex involved in the regulation of cellular responses to DNA damage and proteolytic processes. DDB1, as a component of the DDB1-CUL4-RBX1 E3 ubiquitin ligase complex, plays a pivotal role in recognizing and recruiting substrate proteins for ubiquitination, thereby influencing various cellular pathways, including DNA repair, cell cycle regulation, and signal transduction. DCAF10, a DDB1-CUL4 associated factor, has emerged as a key player in mediating the interaction between the E3 ligase complex and specific substrates, particularly those related to cellular stress responses. Research into the DCAF10-DDB1 complex has gained momentum due to its implications in cancer biology and potential therapeutic applications; it is critical for understanding how cells maintain genomic integrity under stress. Accumulating evidence suggests that dysregulation of this complex may contribute to tumorigenesis, making it a target for therapeutic intervention. Understanding the structural and functional dynamics of DCAF10-DDB1 is essential for elucidating its role in disease mechanisms and developing novel strategies for cancer treatment. Consequently, ongoing studies focus on the molecular interactions, post-translational modifications, and regulatory mechanisms governing this complex, aiming to provide insights that could lead to innovative approaches in combating cancer and other diseases associated with DNA damage response deficiencies. These efforts highlight the importance of DCAF10-DDB1 not only in fundamental biology but also in the development of targeted therapies.
