Analytical Data
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Gene name
RNF128
- Application
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Alternative Names
RNF128；E3 ubiquitin-Protein ligase RNF128
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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
Q8TEB7
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Expression Region
75-183aa
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AA Sequence
SPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAVDIVAIMIGNLKGTKILQSI
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Molecular Weight
18.2 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
RNF128, also known as TRIM21, is a member of the tripartite motif (TRIM) protein family, which plays a crucial role in various cellular processes, including immune response, apoptosis, and the regulation of protein degradation. The increasing interest in RNF128 arises from its involvement in the recognition and ubiquitination of intracellular pathogens, thereby modulating the immune response and contributing to host defense mechanisms. Studies have shown that RNF128 can interact with various viral proteins, facilitating their degradation and influencing the overall antiviral response. Moreover, its dysregulation has been implicated in several diseases, including autoimmune disorders and cancers. Understanding the structure and function of RNF128 is essential for deciphering its role in health and disease. Researchers have been focusing on the recombinant expression of RNF128 to investigate its biochemical properties, identify potential substrates, and explore its therapeutic implications. By studying the recombinant protein, scientists aim to enhance our understanding of its mechanism of action and its potential as a target for novel therapeutics. The continued exploration of RNF128's functions may reveal critical insights into immune regulation and open avenues for innovative treatments against viral infections and malignancies.
