Analytical Data
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基因名
RNF4
- Application
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别名
RES4-26; SNURF; E3 ubiquitin-protein ligase RNF4; Small nuclear ring finger protein
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种属
Mouse
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9QZS2
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表达区间
Met1~Ile194
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分子量
52kDa
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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
RNF4 (RING Finger Protein 4) is a member of the RING finger E3 ubiquitin ligase family, which plays a critical role in the ubiquitin-proteasome system by mediating the tagging of proteins for degradation. This process is essential for regulating various cellular functions, including cell cycle progression, DNA repair, and stress responses. RNF4 specifically recognizes polyubiquitinated proteins, facilitating their ubiquitination and subsequent degradation, which in turn helps maintain cellular homeostasis. Recent studies have highlighted its involvement in several biological processes, such as gene expression regulation and the response to cellular stressors. Moreover, aberrations in RNF4 function have been linked to various diseases, including cancer and neurodegenerative disorders, making it a potential target for therapeutic interventions. The study of recombinant RNF4 protein is crucial for understanding its structure, function, and regulatory mechanisms at both cellular and molecular levels. This research not only provides insights into the role of RNF4 in proteolysis and signaling pathways but also opens avenues for developing novel strategies to exploit RNF4’s activity in disease contexts, thus underscoring its significance in biomedical research.
