Analytical Data
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Gene name
TRIM59
- Application
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Alternative Names
TRIM59; RNF104; TRIM57; TSBF1; Tripartite motif-containing Protein 59; RING finger Protein 104; Tumor suppressor TSBF-1
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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
Q8IWR1
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Expression Region
1-403 aa
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AA Sequence
MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH
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Molecular Weight
73.5 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
TRIM59, a member of the TRIM (Tripartite Motif) protein family, has garnered attention in recent years due to its potential roles in cellular processes such as immune response, cell proliferation, and apoptosis. The TRIM family is characterized by a combination of RING, B-box, and coiled-coil domains, which confer E3 ubiquitin ligase activity, influencing protein stability and degradation pathways. Emerging studies have implicated TRIM59 in various diseases, including cancer and autoimmune disorders, suggesting it might serve as a critical regulator in pathophysiological conditions. Researchers have focused on understanding the specific molecular mechanisms through which TRIM59 exerts its effects on cellular functions, including its interactions with other signaling pathways and its influence on transcriptional regulation. Furthermore, TRIM59's role in modulating the immune response has led to investigations regarding its impact on viral infections and inflammation. Given its diverse functions and implications in health and disease, investigating TRIM59 as a recombinant protein for therapeutic applications could pave the way for innovative strategies in disease intervention and management. As such, elucidating the structure-function relationship of TRIM59, alongside its biological significance, remains a critical area of exploration in current biomedical research.
