| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CTDSPL |
| Uniprot No | O15194-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 82-265aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMKYLLP EVTVLDYGKK CVVIDLDETL VHSSFKPISN ADFIVPVEID GTIHQVYVLK RPHVDEFLQR MGQLFECVLF TASLAKYADP VADLLDRWGV FRARLFRESC VFHRGNYVKD LSRLGRELSK VIIVDNSPAS YIFHPENAVP VQSWFDDMTD TELLDLIPFF EGLSREDDVY SMLHRLCNR |
| 预测分子量 | 24 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CTDSPL重组蛋白的3篇文献示例(内容基于研究领域常见方向，部分信息为示例性概括)：
1. **文献名称**：*"Expression and functional characterization of recombinant human CTDSPL phosphatase in E. coli"*
**作者**：Zhang Y. et al.
**摘要**：本研究成功构建了人源CTDSPL基因的原核表达系统，通过大肠杆菌表达并纯化出重组CTDSPL蛋白。酶活性实验表明，该重组蛋白能特异性催化RNA聚合酶II C端结构域(CTD)的丝氨酸残基去磷酸化，揭示了其在转录调控中的潜在作用。
2. **文献名称**：*"Structural insights into the catalytic mechanism of CTDSPL through X-ray crystallography"*
**作者**：Li H. et al.
**摘要**：通过X射线晶体学解析了重组CTDSPL蛋白的三维结构，发现其活性中心含有保守的金属离子结合位点，并阐明了底物识别和催化反应的分子机制。研究为开发靶向CTDSPL的小分子抑制剂提供了结构基础。
3. **文献名称**：*"CTDSPL interacts with Smad proteins to regulate TGF-β signaling in cancer cells"*
**作者**：Wang X. et al.
**摘要**：利用重组CTDSPL蛋白进行免疫共沉淀实验，发现其与Smad蛋白家族成员存在直接相互作用，并通过去磷酸化修饰调控TGF-β信号通路活性。该研究提示CTDSPL可能在肿瘤发生中发挥抑癌作用。
**注**：以上文献为示例性内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索获取。建议结合具体研究方向补充关键词(如“重组表达”“酶活性”“癌症机制”等)进行精确查询。
CTDSPL (CTD small phosphatase-like) is a member of the FCP/SCP (TFIIF-associating CTD phosphatase/small CTD phosphatase) family, which plays critical roles in regulating RNA polymerase II (Pol II)-mediated transcription. The C-terminal domain (CTD) of Pol II undergoes dynamic phosphorylation cycles during transcription initiation, elongation, and termination. CTDSPL, as a serine/threonine phosphatase, specifically dephosphorylates the Ser5 and Ser7 residues of the CTD heptapeptide repeats, influencing transcriptional termination, RNA processing, and chromatin remodeling.
This protein shares structural homology with other CTD phosphatases, featuring a conserved catalytic domain that enables metal-dependent phosphatase activity. CTDSPL is ubiquitously expressed in human tissues and has been implicated in multiple cellular processes, including cell differentiation, apoptosis, and tumor suppression. Studies link CTDSPL to the TGF-β/BMP signaling pathway, where it dephosphorylates SMAD proteins, modulating their transcriptional activity and downstream gene expression. Dysregulation of CTDSPL has been associated with cancers, such as acute myeloid leukemia and breast cancer, often due to genomic deletions or mutations.
Recombinant CTDSPL proteins are engineered using expression systems like *E. coli* or mammalian cells to produce functional, purified forms for biochemical and functional studies. These proteins are vital for elucidating CTDSPL’s enzymatic mechanisms, substrate interactions, and regulatory networks. Applications include *in vitro* phosphatase assays, structural analysis (e.g., crystallography), and drug discovery targeting CTDSPL-related pathways. Its role as a tumor suppressor also makes recombinant CTDSPL a potential candidate for therapeutic development or biomarker research in oncology. Ongoing studies aim to clarify its tissue-specific functions and therapeutic relevance in human diseases.
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