Analytical Data
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Gene name
RNF130
- Application
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Alternative Names
RNF130
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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
Q86XS8
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Expression Region
28-194 aa
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AA Sequence
DNASQEYYTALINVTVQEPGRGAPLTFRIDRGRYGLDSPKAEVRGQVLAPLPLHGVADHLGCDPQTRFFVPPNIKQWIALLQRGNCTFKEKISRAAFHNAVAVVIYNNKSKEEPVTMTHPGTGDIIAVMITELRGKDILSYLEKNISVQMTIAVGTRMPPKNFSRGS
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Molecular Weight
25.4 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
RNF130, an E3 ubiquitin ligase, plays a crucial role in the regulation of various cellular processes, including the immune response, cell proliferation, and apoptosis. Research into RNF130 has gained momentum due to its implication in several disease states, particularly in cancer and autoimmune disorders. Its function as a regulator of protein stability and turnover highlights its potential as a therapeutic target. Increased levels of RNF130 have been associated with poor prognosis in certain cancers, suggesting that it may promote tumorigenesis by modulating the degradation of key regulatory proteins. Additionally, RNF130 has been shown to influence the activity of cytokines and other molecules involved in immune responses, indicating a broader role in maintaining cellular homeostasis. Understanding the structure and activity of RNF130 through the study of recombinant protein can provide insights into its mechanisms of action, allowing researchers to delineate its role in disease pathology further. This research underscores the importance of RNF130 in both basic cellular functions and disease contexts, thereby opening avenues for novel therapeutic strategies targeting this E3 ligase. Insights gained from RNF130 studies could lead to innovative approaches in manipulating its activity for therapeutic benefits in cancer and other diseases where aberrations in protein turnover are evident. As such, exploring RNF130 as a recombinant protein presents a valuable opportunity to unlock new knowledge about its functional dynamics and regulatory mechanisms in health and disease.
