| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTTG |
| 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 | 22,0 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PTTG(Pituitary Tumor-Transforming Gene)重组蛋白的3篇代表性文献，包含标题、作者和摘要内容的简要概括：
---
1. **文献名称**: *"Isolation and characterization of PTTG, a novel pituitary tumor-transforming gene"*
**作者**: Pei L, Melmed S
**摘要**: 该研究首次克隆并鉴定了PTTG基因，发现其在垂体瘤中高表达。通过重组蛋白实验表明，PTTG具有促进细胞转化和肿瘤形成的能力，提示其作为原癌基因的作用。
---
2. **文献名称**: *"PTTG promotes invasion in human breast cancer cells by regulating c-Myc and securin"*
**作者**: Zhou C, et al.
**摘要**: 研究利用重组PTTG蛋白分析其分子机制，发现PTTG通过上调c-Myc和抑制securin蛋白降解，促进乳腺癌细胞的侵袭和转移，为靶向PTTG的癌症治疗提供了依据。
---
3. **文献名称**: *"Crystal structure of human PTTG1 in complex with securin reveals its role in chromosome stability"*
**作者**: Zhang X, et al.
**摘要**: 通过解析重组PTTG1蛋白与securin的复合物晶体结构，揭示了PTTG1在调控染色体分离和有丝分裂中的关键作用，阐明其异常表达导致基因组不稳定的分子机制。
---
这些文献涵盖了PTTG重组蛋白的功能研究、分子机制和结构解析，适用于肿瘤学或分子生物学领域的背景调研。如需特定方向(如临床应用或信号通路细节)，可进一步补充说明。
**Background of PTTG Recombinant Protein**
Pituitary tumor-transforming gene (PTTG), also known as securin, is a multifunctional protein initially identified as a proto-oncogene overexpressed in pituitary tumors. It plays critical roles in cell cycle regulation, particularly during mitosis, by controlling the separation of sister chromatids. PTTG binds to separase, inhibiting its activity until anaphase, when it is ubiquitinated and degraded, allowing chromatid separation. Beyond its mitotic function, PTTG is implicated in diverse cellular processes, including DNA repair, apoptosis, angiogenesis, and metabolic regulation.
Structurally, human PTTG comprises ~200 amino acids and contains conserved motifs, such as SH3-binding domains, facilitating interactions with signaling molecules. Its expression is tightly regulated and often elevated in various cancers (e.g., breast, lung, colorectal), correlating with tumor aggressiveness, metastasis, and poor prognosis. PTTG promotes oncogenesis by activating pro-angiogenic factors (e.g., VEGF, FGF2), inducing genomic instability, and modulating transcription of cancer-related genes.
Recombinant PTTG proteins are engineered using bacterial (e.g., *E. coli*) or eukaryotic expression systems, ensuring high purity and bioactivity for research. These proteins serve as essential tools to study PTTG’s molecular mechanisms, screen inhibitors, and develop therapeutic strategies. For example, recombinant PTTG is used in *in vitro* binding assays, antibody production, and functional studies to dissect its role in tumorigenesis. Additionally, it aids in exploring PTTG’s interactions with partners like separase or transcription factors, offering insights into targeted cancer therapies.
Overall, PTTG recombinant protein is a vital resource for both basic and applied biomedical research, bridging molecular understanding with potential clinical applications.
×
