Analytical Data
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基因名
RNF114
- Application
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别名
RNF114;ZNF228;ZNF313;E3 ubiquitin-Protein ligase RNF114
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y508
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表达区间
1-228aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSMAAQQRD CGGAAQLAGP AAEADPLGRF TCPVCLEVYE KPVQVPCGHV FCSACLQECL KPKKPVCGVC RSALAPGVRA VELERQIEST ETSCHGCRKN FFLSKIRSHV ATCSKYQNYI MEGVKATIKD ASLQPRNVPN RYTFPCPYCP EKNFDQEGLV EHCKLFHSTD TKSVVCPICA SMPWGDPNYR SANFREHIQR RHRFSYDTFV DYDVDEEDMM NQVLQRSIID Q
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分子量
28 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
RNF114, a member of the RBR E3 ubiquitin ligase family, has garnered significant attention in recent years due to its pivotal role in cellular processes such as protein degradation, signal transduction, and immune responses. Research has revealed that RNF114 is involved in the ubiquitination of specific target proteins, which is crucial for maintaining cellular homeostasis and regulating various biological functions. Its expression is highly regulated and often linked to various diseases, including cancer and autoimmune disorders. Scientists are particularly interested in understanding the molecular mechanisms by which RNF114 exerts its functions and how its dysregulation can lead to pathological conditions. Additionally, the development of recombinant RNF114 proteins allows for an in-depth exploration of its enzymatic activity and substrate specificity, facilitating the identification of potential therapeutic targets. By elucidating the structure-function relationship of RNF114, researchers aim to uncover novel insights that could inform strategies for intervention in diseases associated with its dysfunction. This growing body of research emphasizes the importance of RNF114 in both basic biological research and its potential implications in the field of medicine, thus highlighting the need for continued study of this intriguing protein.
