Analytical Data
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Gene name
RNF126
- Application
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Alternative Names
RING finger protein 126
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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
Q9BV68
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Expression Region
2-311 aa
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AA Sequence
AEASPHPGRYFCHCCSVEIVPRLPDYICPRCESGFIEELPEETRSTENGSAPSTAPTDQSRPPLEHVDQHLFTLPQGYGQFAFGIFDDSFEIPTFPPGAQADDGRDPESRRERDHPSRHRYGARQPRARLTTRRATGRHEGVPTLEGIIQQLVNGIITPATIPSLGPWGVLHSNPMDYAWGANGLDAIITQLLNQFENTGPPPADKEKIQALPTVPVTEEHVGSGLECPVCKDDYALGERVRQLPCNHLFHDGCIVPWLEQHDSCPVCRKSLTGQNTATNPPGLTGVSFSSSSSSSSSSSPSNENATSNS
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Molecular Weight
40.6 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
RNF126 is an E3 ubiquitin ligase that plays a significant role in various cellular processes, including protein degradation, cell cycle regulation, and DNA damage response. Its importance in tumor biology has garnered attention, as altered expression of RNF126 has been implicated in several types of cancers, suggesting it may serve as a potential biomarker or therapeutic target. Research has shown that RNF126 can regulate the stability of multiple substrates, influencing pathways critical for cell proliferation and survival. Moreover, its involvement in the modulation of the NF-kB signaling pathway, known for its role in inflammation and cancer progression, highlights its dual function in normal physiology and disease. Given these roles, the production of recombinant RNF126 protein is essential for studying its biochemical properties and understanding the underlying mechanisms of its action. By utilizing techniques such as protein purification and functional assays, researchers aim to elucidate the precise molecular interactions and pathways in which RNF126 is involved. This understanding could pave the way for developing strategies aimed at manipulating RNF126's function for therapeutic purposes, contributing to more effective cancer treatments and improved patient outcomes. The study of RNF126, therefore, not only provides insights into fundamental biological processes but also holds potential for advancements in targeted cancer therapies.
