Analytical Data
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Gene name
UBR4
- Application
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Alternative Names
UBR4；KIAA0462；KIAA1307；RBAF600；E3 ubiquitin-Protein ligase UBR4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5T4S7
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Expression Region
94-190aa
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AA Sequence
full
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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
Related Products
Protein Description
UBR4, or Ubiquitin Protein Ligase E3 Component N-Recognin 4, is a crucial component in the ubiquitin-proteasome system, which governs protein degradation and maintains cellular homeostasis. Research has shown that UBR4 is involved in regulating the stability and turnover of various substrates, including those connected to critical cellular processes such as cell cycle regulation, DNA damage response, and transcriptional control. Its role in these pathways suggests that UBR4 may influence tumorigenesis and other diseases where protein misfolding and dysregulated degradation are prominent. Additionally, UBR4's involvement in neurodegenerative disorders has been a focus of study, as aberrant protein accumulation can lead to toxicity and neuronal damage. Advances in biotechnological methods, including recombinant protein expression and purification, have enabled more detailed investigations of UBR4's structure and function. Understanding UBR4's precise mechanisms could provide insights into its potential as a therapeutic target and lead to the development of novel treatments for diseases related to protein mismanagement. Overall, ongoing research into UBR4 highlights its significance in cellular regulation and the potential for therapeutic innovations in disease management.
