Analytical Data
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Gene name
RNF11
- Application
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Alternative Names
RNF11；RING finger Protein 11
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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
Q9Y3C5
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Expression Region
2-154aa
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AA Sequence
GNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPVYHPTPSQTRLATQLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHIYHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN
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Molecular Weight
19.3 kDa
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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
RNF11 (Ring Finger Protein 11) is an E3 ubiquitin ligase that plays a crucial role in cellular processes such as protein degradation, signal transduction, and cell cycle regulation. Its involvement in these processes has attracted significant interest in the context of various diseases, including cancer and neurodegenerative disorders. Recent studies have shown that RNF11 can regulate the stability of key oncogenic proteins, suggesting its potential as a therapeutic target in tumorigenesis. Furthermore, RNF11 is implicated in the modulation of immune responses, highlighting its importance in both innate and adaptive immunity. Despite its significance, the detailed molecular mechanisms by which RNF11 exerts its functions remain largely unclear. To investigate the functional roles of RNF11, recombinant protein studies have emerged as a powerful approach to elucidate its interactions and activities in cellular contexts. Through the production and purification of RNF11 recombinant proteins, researchers aim to delineate its biochemical properties, binding partners, and the pathways it influences. This research not only provides insights into the biological functions of RNF11 but also opens avenues for the development of novel therapeutic strategies aimed at modulating its activity in disease states. Therefore, the study of RNF11 recombinant proteins is of paramount importance in understanding both fundamental cellular biology and the potential for targeted interventions in disease treatment.
