Analytical Data
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Gene name
CUL3-RBX1
- Application
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Alternative Names
KIAA0617; Cullin-4A
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Species
Human
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Source
Baculovirus
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Tag
N-StrepⅡ;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13618 (S2-A768)&P62877
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Expression Region
Q13618 (S2-A768)&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
CUL3-RBX1 is a critical component of the ubiquitin-proteasome system, which plays a vital role in regulating protein degradation and cellular homeostasis. CUL3 (Cullin-3) serves as a scaffold protein that assembles E3 ubiquitin ligase complexes, while RBX1 (RING-box protein 1) functions as the RING domain that facilitates the transfer of ubiquitin from E2 conjugating enzymes to target substrates. The CUL3-RBX1 complex is involved in various biological processes, including cell cycle progression, signal transduction, and response to stress. Dysregulation of this complex has been implicated in numerous diseases, particularly cancer, where aberrant degradation of key regulatory proteins can drive oncogenesis. Recent studies have revealed that the CUL3-RBX1 axis can modulate the stability of several transcription factors and tumor suppressors, further highlighting its relevance in tumor biology. Understanding the mechanistic details of CUL3-RBX1 interactions and its substrate specificity is essential, as it opens avenues for the development of targeted therapeutics aimed at modulating its activity. Exploring the potential of CUL3-RBX1 as a therapeutic target could lead to novel strategies in cancer treatment and provide insights into harnessing the ubiquitin-proteasome system for therapeutic purposes.
