| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Tacstd1 |
| Uniprot No | P16422 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-265aa |
| 氨基酸序列 | QEECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEM NGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSTCWCVNTAG VRRTDKDTEITCSERVRTYWIIIELKHKAREKPYDSKSLRTALQKEITTR YQLDPKFITSILYENNVITIDLVQNSSQKTQNDVDIADVAYYFEKDVKGE SLFHSKKMDLTVNGEQLDLDPGQTLIYYVDEKAPEFSMQGLKVDHHHHHH |
| 预测分子量 | 28 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TACSTD1(TROP1/EpCAM)重组蛋白的3篇参考文献示例，格式包含文献名称、作者及简要摘要内容：
---
1. **"Recombinant TROP1 extracellular domain inhibits tumor growth by blocking epithelial-mesenchymal transition in colorectal cancer"**
*Zhang Y, et al. (2020).*
摘要：研究通过在大肠杆菌中表达TACSTD1胞外域重组蛋白，发现其能抑制结直肠癌细胞上皮-间质转化(EMT)，降低肿瘤侵袭性，为靶向治疗提供新策略。
2. **"Structural characterization of EpCAM extracellular domain using recombinant protein produced in HEK293 cells"**
*Lee S, et al. (2018).*
摘要：利用HEK293细胞表达并纯化EpCAM(TACSTD1)胞外区重组蛋白，通过X射线晶体学解析其三维结构，揭示其介导细胞黏附的分子机制。
3. **"Development of a TACSTD1-based recombinant protein vaccine targeting cancer stem cells"**
*Wang H, et al. (2019).*
摘要：构建基于TACSTD1重组蛋白的肿瘤疫苗，实验显示其可诱导特异性抗体反应，抑制小鼠模型中癌症干细胞的增殖和转移。
---
**备注**：上述文献为示例，实际引用时需核实具体来源及准确性。若需真实文献，建议通过PubMed或Web of Science以“TACSTD1 recombinant protein”或“EpCAM recombinant”为关键词检索近年研究。
Tacstd1 (tumor-associated calcium signal transducer 1), also known as TROP2 or TACSTD2. is a transmembrane glycoprotein encoded by the TACSTD1 gene. Initially identified as a tumor-associated antigen, it is overexpressed in numerous epithelial-derived cancers, including breast, lung, pancreatic, and colorectal cancers, while showing limited expression in normal tissues. Structurally, Tacstd1 consists of an extracellular domain with cysteine-rich motifs, a transmembrane region, and a short cytoplasmic tail harboring signaling motifs. Its interaction with intracellular pathways, such as MAPK/ERK and PI3K/AKT, contributes to its role in promoting cell proliferation, migration, and metastasis. Dysregulation of Tacstd1 is closely linked to poor prognosis and therapeutic resistance, making it a compelling biomarker and therapeutic target.
Recombinant Tacstd1 protein, produced via expression systems like mammalian or bacterial cells, retains the functional epitopes of the native protein. This engineered protein is widely utilized in biochemical assays, antibody development, and structural studies to elucidate its role in cancer biology. For instance, it serves as an antigen for generating anti-TROP2 antibodies used in diagnostic immunohistochemistry or therapeutic agents like antibody-drug conjugates (ADCs). Notably, the FDA-approved ADC sacituzumab govitecan targets Tacstd1. highlighting its clinical relevance. Researchers also employ recombinant Tacstd1 to study its interaction with ligands or signaling partners, shedding light on mechanisms driving tumor progression. Additionally, it aids in exploring Tacstd1's potential in targeted drug delivery systems due to its cancer-specific expression. Despite its established oncogenic role, emerging studies suggest context-dependent functions in tissue repair and stem cell regulation, necessitating further investigation. Overall, recombinant Tacstd1 remains a critical tool for advancing both basic research and translational applications in oncology.
×
