Analytical Data
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Gene name
CRBN-DDB1-CUL4A-RBX1 Complex
- Application
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Alternative Names
Cereblon-DDB1-Cul4A-Rbx1 Complex
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Species
Human
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Source
Baculovirus
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Tag
N-His;N-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96SW2-1 (M1-L442)&Q16531-1 (M1-H1140)&Q13619-1 (A2-A759)&P62877
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Expression Region
Q96SW2-1 (M1-L442)&Q16531-1 (M1-H1140)&Q13619-1 (A2-A759)&P62877 (M1-H108)
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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
The CRBN-DDB1-CUL4A-RBX1 complex, a pivotal component of the cullin-RING E3 ubiquitin ligase system, plays a crucial role in the regulation of protein degradation through the ubiquitin-proteasome pathway. This multi-subunit complex is essential for various cellular processes, including cell cycle regulation, DNA repair, and the response to oxidative stress. The CRBN (Cerberus and Docking protein 1) subunit is particularly important due to its role in substrate recognition and specificity, as it interacts with DDB1 (Damage-Specific DNA Binding Protein 1), which serves as a molecular scaffold, linking substrates to the cullin-RING E3 ligase machinery. CUL4A (Cullin 4A) functions as a scaffold protein, while RBX1 (RING-box protein 1) acts as the RING-type finger that recruits ubiquitin-conjugating enzymes to facilitate ubiquitination. Dysregulation of this complex has been implicated in various diseases, including cancer, making it a potential therapeutic target. Recent advancements in structural biology and biochemistry have provided insights into the molecular architecture and dynamics of the CRBN-DDB1-CUL4A-RBX1 complex, paving the way for the development of small-molecule inhibitors that could modulate its activity. Understanding the precise mechanisms by which this complex regulates protein turnover and signal transduction could reveal new strategies for treating diseases linked to the ubiquitin-proteasome pathway. The ongoing research in this realm aims to elucidate the complex's substrate specificity and the intricate signaling networks it governs, which is essential for developing efficient therapeutic interventions.
