Analytical Data
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Gene name
RNF125
- Application
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Alternative Names
RING finger protein 125 T-cell RING activation protein 1
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96EQ8
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Expression Region
1-232aa
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Molecular Weight
53.3 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
RNF125 is an E3 ubiquitin ligase identified as a key regulator in various cellular processes, including immune response, cell proliferation, and apoptosis. Research has shown that RNF125 plays a significant role in modulating the signaling pathways of several important proteins, such as NF-κB and p53, thereby influencing tumorigenesis and the body's defense mechanisms against viral infections. Its involvement in the ubiquitin-proteasome system highlights its potential as a therapeutic target for various diseases, including cancer and autoimmune disorders. The study of recombinant RNF125 protein has garnered attention as recombinant techniques allow for the production of large quantities of the protein for functional assays and structural analyses, enhancing our understanding of its molecular mechanisms. Characterizing RNF125’s enzymatic activity and identifying its substrates could unveil new insights into its role in disease pathology and provide opportunities for the development of novel therapeutic strategies. Furthermore, exploring the modulation of RNF125 activity may lead to innovative approaches in treating conditions linked to dysregulated ubiquitination. Ongoing research aims to elucidate the precise biological functions of RNF125 and its potential as a biomarker for disease progression or a target for drug development, marking its importance in both basic research and clinical applications.
