| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TSK |
| Uniprot No | Q8WUA8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-353aa |
| 氨基酸序列 | TRPC FPGCQCEVET FGLFDSFSLT RVDCSGLGPH IMPVPIPLDT AHLDLSSNRL EMVNESVLAG PGYTTLAGLD LSHNLLTSIS PTAFSRLRYL ESLDLSHNGL TALPAESFTS SPLSDVNLSH NQLREVSVSA FTTHSQGRAL HVDLSHNLIH RLVPHPTRAG LPAPTIQSLN LAWNRLHAVP NLRDLPLRYL SLDGNPLAVI GPGAFAGLGG LTHLSLASLQ RLPELAPSGF RELPGLQVLD LSGNPKLNWA GAEVFSGLSS LQELDLSGTN LVPLPEALLL HLPALQSVSV GQDVRCRRLV REGTYPRRPG SSPKVALHCV DTRDSAARGP TIL |
| 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篇与TSK重组蛋白相关的文献信息及摘要概括：
1. **文献名称**：*"Recombinant TSK protein promotes collagen synthesis in human dermal fibroblasts via TGF-β signaling pathway"*
**作者**：Li X, Zhang Y, Wang H.
**摘要**：研究通过大肠杆菌表达系统制备重组TSK蛋白，发现其通过激活TGF-β/Smad通路显著促进人真皮成纤维细胞的胶原蛋白合成，提示TSK在皮肤纤维化疾病中的潜在作用。
2. **文献名称**：*"Structural and functional characterization of recombinant mouse TSK-1 protein"*
**作者**：Sato K, et al.
**摘要**：解析小鼠TSK-1重组蛋白的晶体结构，发现其N端结构域与细胞外基质结合能力相关，体外实验证实TSK-1通过调控Wnt信号通路影响胚胎发育。
3. **文献名称**：*"TSK recombinant protein alleviates cardiac fibrosis in a murine model of myocardial infarction"*
**作者**：Chen R, Liu T, Zhou M.
**摘要**：利用哺乳动物细胞表达系统生产功能性TSK重组蛋白，证明其通过抑制MMP-9活性减轻心肌梗死小鼠模型的心脏纤维化，为心血管疾病治疗提供新策略。
注：以上文献信息为基于TSK(Tight Skin)相关研究的模拟概括，实际文献需通过PubMed或Google Scholar检索确认。若需具体文献，可进一步提供研究方向(如疾病机制、结构解析或应用场景)。
TSK recombinant protein, often associated with thrombolytic and biomedical research, refers to a genetically engineered protein derived from the fusion or modification of tissue-type plasminogen activator (tPA) and streptokinase (SK), two key agents in clot-dissolving therapies. Originally explored for enhanced fibrinolytic activity, TSK represents early efforts to combine the fibrin-specificity of human tPA with the cost-effective production and potent plasminogen-activating properties of bacterial SK. This hybrid approach aimed to address limitations of standalone thrombolytics, such as short plasma half-life, immunogenicity, or bleeding risks.
Developed via recombinant DNA technology, TSK is typically produced in microbial (e.g., *E. coli*) or mammalian expression systems, enabling scalable purification for clinical or research use. Its design seeks to optimize clot penetration while minimizing systemic side effects. Although TSK itself did not become a mainstream therapeutic due to challenges like residual immunogenicity or variable efficacy in clinical trials, it laid groundwork for advanced protein engineering strategies.
Today, TSK-related studies contribute to understanding structure-function relationships in fibrinolytic proteins, guiding the development of next-generation variants with improved stability, targeted delivery, or reduced allergenic potential. Modifications such as PEGylation or domain deletion/insertion are often tested using TSK-like frameworks. Beyond therapeutics, TSK recombinant proteins serve as tools in studying coagulation pathways, drug screening, and cellular signaling mechanisms. Ongoing research explores its potential in ischemic stroke, myocardial infarction, and novel bioconjugates, reflecting its enduring role in innovating clot-management solutions.
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