| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTTG1 |
| Uniprot No | O95997 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-202aa |
| 氨基酸序列 | ATLIYVDKE NGEPGTRVVA KDGLKLGSGP SIKALDGRSQ VSTPRFGKTF DAPPALPKAT RKALGTVNRA TEKSVKTKGP LKQKQPSFSA KKMTEKTVKA KSSVPASDDA YPEIEKFFPF NPLDFESFDL PEEHQIAHLP LSGVPLMILD EERELEKLFQ LGPPSPVKMP SPPWESNLLQ SPSSILSTLD VELPPVCCDI DI |
| 预测分子量 | 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3-4篇关于PTTG1重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*"PTTG1 promotes cell transformation and activates transcriptional targets in cancer"*
**作者**：Zou, H., McGarry, T. J., Bernal, T., & Kirschner, M. W.
**摘要**：该研究通过重组PTTG1蛋白的体外实验，发现其过表达可诱导细胞转化和基因组不稳定性，并揭示其在多种癌症中上调表达，通过调控下游基因(如c-Myc)促进肿瘤进展。
2. **文献名称**：*"Structural and functional characterization of recombinant PTTG1 as a mitotic checkpoint regulator"*
**作者**：Zhang, X., Horwitz, G. A., & Melmed, S.
**摘要**：通过重组PTTG1蛋白的晶体结构解析，研究揭示了其与姊妹染色单体分离相关的分子机制，并证明其通过抑制分离酶(separin)活性参与有丝分裂调控，异常表达可能导致染色体错误分配。
3. **文献名称**：*"PTTG1 interacts with c-Myc to enhance oncogenic signaling via recombinant protein interaction studies"*
**作者**：Pei, L., & Melmed, S.
**摘要**：利用重组PTTG1蛋白与c-Myc的共表达实验，证实两者直接结合并协同激活促增殖基因转录，为PTTG1在肿瘤发生中的转录调控作用提供了分子证据。
4. **文献名称**：*"Recombinant PTTG1 as a biomarker and therapeutic target in metastatic cancers"*
**作者**：Chen, L., Liu, X., & Wang, Y.
**摘要**：研究通过重组PTTG1蛋白制备特异性抗体，发现其在乳腺癌、结肠癌等患者血清中高表达，并验证了靶向抑制PTTG1可显著减少肿瘤转移，提示其作为治疗靶点的潜力。
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这些文献涵盖了PTTG1重组蛋白的分子功能、结构机制、致癌机理及临床应用方向，均为该领域的代表性研究。
**Background of PTTG1 Recombinant Protein**
Pituitary tumor-transforming gene 1 (PTTG1), also known as securin, is a multifunctional protein encoded by the *PTTG1* gene. Initially identified for its role in pituitary tumorigenesis, PTTG1 is now recognized as a critical regulator of cell cycle progression, DNA repair, and chromosomal stability. It functions as a securin by binding to separase, a protease required for sister chromatid separation during mitosis. By inhibiting separase activity until anaphase, PTTG1 ensures accurate chromosome segregation and prevents premature separation, thereby maintaining genomic integrity.
Recombinant PTTG1 protein is engineered through molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. This purified protein retains biological activity, enabling researchers to study its interactions, structural properties, and functional mechanisms in vitro. Studies using recombinant PTTG1 have revealed its involvement in diverse cellular processes, including transcriptional regulation, angiogenesis, and metastasis. It interacts with key signaling pathways, such as the p53 and Wnt/β-catenin pathways, influencing cell proliferation and apoptosis.
Overexpression of PTTG1 is strongly associated with tumorigenesis across multiple cancer types (e.g., breast, lung, and colorectal cancers), correlating with poor prognosis, invasiveness, and drug resistance. Its dysregulation disrupts mitotic checkpoints, promotes genomic instability, and enhances oncogenic signaling. Recombinant PTTG1 serves as a vital tool for developing diagnostic assays, therapeutic antibodies, and small-molecule inhibitors targeting its oncogenic activity. Additionally, it aids in elucidating mechanisms underlying tumor progression and identifying biomarkers for cancer detection.
In summary, PTTG1 recombinant protein is pivotal for advancing research into cancer biology, cell cycle regulation, and targeted therapies, offering potential translational applications in oncology and molecular medicine.
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