Analytical Data
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Gene name
CUL4A-RBX1
- Application
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Alternative Names
Cullin-4A; CUL4A; Homo sapiens; Human
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13619-1 (A2-A759)&P62877
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Expression Region
Q13619-1 (A2-A759)&P62877 (M1-H108)
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Molecular Weight
87.6 KDa/12.2 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
CUL4A-RBX1 is an important component of the Cullin-RING E3 ubiquitin ligase complex, which plays a critical role in regulating protein degradation and various cellular processes, including cell cycle progression, DNA repair, and response to stress. The CUL4A protein serves as a scaffold for the assembly of the E3 ligase complex, while RBX1 acts as the RING finger protein, facilitating the transfer of ubiquitin to target substrates. Dysregulation of the CUL4A-RBX1 complex has been implicated in various diseases, particularly cancer, as it can lead to the aberrant accumulation of proteins that drive tumorigenesis. Research on the CUL4A-RBX1 recombinant protein has focused on understanding its structural characteristics and functional mechanisms, which are essential for developing targeted therapies that can modulate its activity. By elucidating the role of CUL4A-RBX1 in cellular ubiquitination processes, scientists aim to identify novel therapeutic strategies to combat cancer and other diseases associated with misregulated protein homeostasis. Recent studies have also explored the potential of CUL4A-RBX1 as a biomarker for disease progression and prognosis, highlighting its relevance in translational research. Overall, the investigation of CUL4A-RBX1 recombinant protein not only enhances our understanding of the ubiquitin-proteasome system but also opens new avenues for therapeutic interventions in malignancies and other disorders linked to E3 ligase dysfunction.
