Analytical Data
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Gene name
RNF150
- Application
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Alternative Names
RNF150; KIAA1214; RING finger protein 150
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9ULK6
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Expression Region
1-314 aa
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AA Sequence
MASSAHDRLACDPNTKFAAPTRGKNWIALIPKGNCTYRDKIRNAFLQNASAVVIFNVGSNTNETITMPHAGVEDIVAIMIPEPKGKEIVSLLERNITVTMYITIGTRNLQKYVSRTSVVFVSISFIVLMIISLAWLVFYYIQRFRYANARDRNQRRLGDAAKKAISKLQIRTIKKGDKETESDFDNCAVCIEGYKPNDVVRILPCRHLFHKSCVDPWLLDHRTCPMCKMNILKALGIPPNADCMDDLPTDFEGSLGGPPTNQITGASDTTVNESSVTLDPAVRTVGALQVVQDTDPIPQEGDVIFTTNSEFCHT
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Molecular Weight
61.3 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
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Protein Description
RNF150, an E3 ubiquitin ligase, has garnered considerable attention in the field of molecular biology due to its critical role in cellular signaling and regulatory pathways. Its involvement in various biological processes, including immune response and cell proliferation, highlights its significance in maintaining cellular homeostasis. Emerging evidence suggests that RNF150 is implicated in the regulation of oncogenic pathways, potentially influencing cancer development and progression. Researchers have noted its unique structural features, which facilitate the transfer of ubiquitin moieties to target proteins, thereby modulating their stability and activity. The study of RNF150's recombinant protein has paved the way for a deeper understanding of its enzymatic functions and interactions with other cellular components. By producing RNF150 in a recombinant form, scientists are able to conduct in vitro studies to elucidate its molecular mechanisms and identify potential substrates. This line of research not only enhances our comprehension of RNF150's role in cancer biology but also opens opportunities for therapeutic interventions targeting this E3 ligase. Given its critical functions, further exploration of RNF150’s dynamics and its implications in health and disease remains a promising avenue for future investigation.
