Analytical Data
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Gene name
CUL5-RBX1
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简介
The CUL5 protein is a core component of the SCF-like ECS E3 ubiquitin-protein ligase complex. CUL5/RBX1 Protein, Human (Active, Sf9, His, Strep) is the recombinant human-derived CUL5/RBX1, expressed by Sf9 insect cells, with Strep, His labeled tag.
- Application
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Alternative Names
VACM1
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Species
Human
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Source
Baculovirus
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Tag
His;N-StrepⅡ
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q93034 (A2-A780)&P62877
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Expression Region
Q93034 (A2-A780)&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
CUL5-RBX1 is a critical component of the E3 ubiquitin ligase complex, which plays a significant role in the ubiquitin-proteasome system responsible for protein degradation and regulation of various cellular processes. CUL5 (Cullin 5) acts as a scaffolding protein that allows for the recruitment of substrate-adapter proteins, while RBX1 (Ring Box 1) serves as the RING finger protein essential for the ubiquitin transfer function. Dysregulation of this complex has been implicated in various diseases, including cancer, due to its influence on the stability and turnover of key regulatory proteins involved in cell cycle progression, apoptosis, and signal transduction. Recent studies have focused on elucidating the structural and functional dynamics of CUL5-RBX1 to understand how modifications and interactions with different substrate adaptors can alter its activity. These insights could pave the way for novel therapeutic strategies aimed at targeting aberrant E3 ligase activity in disease contexts. Researchers are particularly interested in the potential of modulating the CUL5-RBX1 complex to restore normal cellular function and combat tumorigenesis. Understanding the mechanisms governing CUL5-RBX1 interactions and their downstream effects on substrate proteins is essential for developing interventions that leverage the ubiquitin-proteasome system's regulatory capabilities.
