Analytical Data
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Gene name
CUL2-RBX1
- Application
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Alternative Names
Cullin-2; CUL2; Homo sapiens; Human; CUL-2
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Species
Human
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Source
Baculovirus
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13617 (M1-A745)&P62877
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Expression Region
Q13617 (M1-A745)&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
CUL2-RBX1 is a critical component of the cullin-RING ubiquitin ligase (CRL) family, which plays a vital role in regulating protein homeostasis by mediating the ubiquitination and subsequent proteasomal degradation of target proteins. Understanding the function of CUL2-RBX1 is essential as it is involved in various cellular processes, including cell cycle regulation, signal transduction, and responses to stress. Dysregulation of this ubiquitin ligase has been implicated in several diseases, particularly cancer, where abnormal protein degradation can lead to tumorigenesis. CUL2 functions as a scaffolding protein that assembles with various substrates and adaptors, allowing for substrate specificity. RBX1, as the RING-finger component, is crucial for transferring ubiquitin from the E2 ubiquitin-conjugating enzymes to substrate proteins. Recent studies have focused on the structural and functional characterization of the CUL2-RBX1 complex, seeking to elucidate its mechanistic role in ubiquitin-mediated pathways and identify potential therapeutic targets. Advancements in techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into the complex's architecture, revealing how substrate recognition and ubiquitin transfer are regulated. As research progresses, CUL2-RBX1 continues to be a target of interest for developing novel cancer therapies that exploit the ubiquitin-proteasome system to restore normal protein turnover in diseased cells. Understanding the interplay between CUL2-RBX1 and its substrates is crucial for unraveling the complexities of cellular regulation and therapeutic intervention.
