Analytical Data
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基因名
RNF152
- Application
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别名
RNF152; E3 ubiquitin-protein ligase RNF152; RING finger protein 152; RING-type E3 ubiquitin transferase RNF152
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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
Q8N8N0
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表达区间
1-203 aa
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氨基酸序列
METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGVTKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG
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分子量
48.8 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
RNF152, a member of the RING finger protein family, has gained increasing attention in recent years due to its potential role in various biological processes and diseases. This E3 ubiquitin ligase is involved in regulating protein degradation, cellular signaling pathways, and immune responses, making it a critical player in maintaining cellular homeostasis. Research has suggested that RNF152 may be implicated in tumorigenesis and the progression of certain cancers, as its dysregulation can lead to aberrant protein accumulation and altered cellular functions. Furthermore, RNF152 is thought to participate in the modulation of inflammation and immune responses, with potential implications for autoimmune diseases. The expression and activity of RNF152 can be influenced by various stressors, highlighting its role as a regulator of cellular responses to environmental changes. Given its multifaceted functions, understanding the mechanisms underlying RNF152’s actions could provide valuable insights into therapeutic targets for treating diseases associated with its dysregulation. Consequently, studies focusing on the recombinant production of RNF152 are essential for elucidating its structure-function relationship, regulatory mechanisms, and potential applications in drug development and therapeutic interventions.
