Analytical Data
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基因名
TRIM59
- Application
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别名
TRIM59; RNF104; TRIM57; TSBF1; Tripartite motif-containing Protein 59; RING finger Protein 104; Tumor suppressor TSBF-1
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8IWR1
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表达区间
1-403 aa
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氨基酸序列
MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH
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分子量
73.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
