Analytical Data
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Gene name
RNF181
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简介
RNF181 Protein, an E3 ubiquitin-protein ligase, mediates the monoubiquitination of the 26S proteasome subunit PSMC2/RPT1. This suggests a role in regulating the 26S proteasome, a vital cellular machinery for protein degradation. RNF181's capacity to modulate PSMC2/RPT1 implies involvement in the intricate regulatory network governing cellular protein homeostasis. RNF181 Protein, Human (His) is the recombinant human-derived RNF181 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
RNF181; E3 ubiquitin-protein ligase RNF181; RING finger protein 181
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9P0P0
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Expression Region
A2-T153
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Protein Length
Partial
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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
RNF181 is a member of the RING finger protein family, which plays a critical role in various cellular processes, including protein ubiquitination, signal transduction, and the regulation of gene expression. Recent studies have highlighted its significance in the modulation of immune responses and potential involvement in tumorigenesis. The reconstitution of RNF181 as a recombinant protein allows for detailed biochemical and biophysical characterization, enabling researchers to explore its specific functions and interactions at a molecular level. Understanding the structure-function relationship of RNF181 is vital, as it may reveal new insights into how dysregulation of this protein contributes to disease mechanisms, especially in cancers where E3 ubiquitin ligases are often implicated. Furthermore, RNF181 has been suggested as a potential therapeutic target, making its study particularly relevant in the context of drug development and personalized medicine. By utilizing recombinant technologies, scientists can produce RNF181 in a controlled environment, facilitating the exploration of its role in cellular pathways and its potential as a biomarker for diseases. Overall, the investigation of RNF181 as a recombinant protein paves the way for advancements in both basic and applied biomedical research.
