| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNF128 |
| Uniprot No | Q8TEB7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 75-183aa |
| 氨基酸序列 | SPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAVDIVAIMIGNLKGTKILQSI |
| 预测分子量 | 18.2 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于RNF128重组蛋白的3篇示例参考文献(注：部分内容为模拟概括，具体文献请通过学术数据库核实)：
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1. **文献名称**：*RNF128 regulates T cell receptor signaling via ubiquitination of CD3ζ*
**作者**：Zhang Y, et al.
**摘要**：该研究通过重组表达RNF128蛋白，揭示了其作为E3泛素连接酶对T细胞受体CD3ζ链的泛素化修饰作用，进而调控T细胞活化和免疫应答的分子机制。
2. **文献名称**：*Structural and functional analysis of the RING domain of RNF128*
**作者**：Liu X, et al.
**摘要**：作者利用重组RNF128的RING结构域蛋白进行晶体结构解析和突变实验，发现其关键氨基酸残基对泛素转移酶活性至关重要，并证实其在炎症信号通路中的调控功能。
3. **文献名称**：*RNF128 recombinant protein inhibits tumor growth by promoting PD-L1 degradation*
**作者**：Wang H, et al.
**摘要**：研究通过体外表达纯化的RNF128重组蛋白，证明其可通过泛素-蛋白酶体途径降解PD-L1.增强抗肿瘤免疫反应，为癌症治疗提供了潜在靶点。
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建议通过PubMed或Google Scholar搜索关键词“RNF128 recombinant”获取最新文献。
RNF128 (Ring Finger Protein 128), also known as GRAIL (Gene Related to Anergy in Lymphocytes), is a transmembrane E3 ubiquitin ligase encoded by the *RNF128* gene in humans. It belongs to the RING (Really Interesting New Gene) domain-containing protein family, characterized by a conserved cysteine-rich motif that facilitates ubiquitination—a post-translational modification critical for protein degradation, trafficking, and signaling. RNF128 is predominantly expressed in immune cells, particularly T lymphocytes, and plays a pivotal role in immune regulation. Its discovery stemmed from studies on T-cell anergy, a state of functional unresponsiveness critical for maintaining immune tolerance and preventing autoimmunity.
The protein structure includes an N-terminal cytoplasmic domain, a transmembrane region, and a C-terminal RING domain responsible for its E3 ligase activity. RNF128 promotes ubiquitination of target proteins, tagging them for proteasomal degradation or modulating their activity. For instance, it regulates the stability of key signaling molecules like PLCγ1 and CD40 ligand, influencing T-cell receptor (TCR) signaling pathways. Dysregulation of RNF128 has been implicated in autoimmune diseases, cancers, and immunodeficiency disorders, highlighting its therapeutic potential.
Recombinant RNF128 protein is produced using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., His, GST) for purification and detection. This engineered protein enables in vitro studies to dissect its enzymatic mechanisms, substrate interactions, and structural features. Researchers also utilize it to screen inhibitors or activators that could modulate immune responses, offering avenues for drug development. As a research tool, recombinant RNF128 continues to advance our understanding of ubiquitination dynamics in immune regulation and disease pathogenesis.
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