| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPS |
| Uniprot No | O60704 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-377aa |
| 氨基酸序列 | MRLSVRRVLLAAGCALVLVLAVQLGQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQLGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSSHLGSS |
| 预测分子量 | 41,9 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TPS(以Thrombospondin为例)重组蛋白的参考文献示例(注：文献为假设性概括，仅作格式参考)：
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1. **《Recombinant Thrombospondin-1 Suppresses Angiogenesis in Experimental Tumors》**
*作者：Lawler, J., et al.*
摘要：研究通过大肠杆菌表达重组TSP-1蛋白，验证其抑制肿瘤血管生成的作用，动物实验显示其显著减缓小鼠肿瘤生长。
2. **《Expression and Functional Characterization of Recombinant TSP-2 in Wound Healing》**
*作者：Kyriakides, T.R., et al.*
摘要：利用哺乳动物细胞系统表达重组TSP-2蛋白，证明其通过调控细胞外基质重塑加速糖尿病小鼠模型中的伤口愈合。
3. **《Optimization of Recombinant TPS Production in Pichia pastoris for Biomedical Applications》**
*作者：Zhang, Y., et al.*
摘要：比较毕赤酵母与大肠杆菌表达系统的重组TSP-1产量及活性，证实酵母系统产出的蛋白糖基化修饰更优，适用于药物递送研究。
4. **《Role of Recombinant TPS in Plant Stress Tolerance: A Structural Analysis》**
*作者：Avonce, N., et al.*
摘要：从拟南芥中克隆TPS基因并在原核系统中表达，解析其晶体结构，揭示其通过海藻糖合成增强植物抗旱能力的分子机制。
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提示：实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。若需真实文献，建议补充具体研究背景(如TPS的全称或应用领域)。
**Background of TPS Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine. Among these, TPS (Tresperimus-binding protein or related targets, context-dependent) recombinant proteins represent a class designed for specific therapeutic or industrial applications. Their development stems from advances in molecular cloning, expression systems, and protein purification techniques.
TPS proteins often derive from naturally occurring molecules modified to enhance stability, solubility, or functionality. For example, in immunotherapy, TPS may refer to engineered proteins targeting immune checkpoints or cellular pathways. In industrial enzymes, thermophilic or pH-resistant TPS variants are optimized for harsh processes.
A key driver for TPS recombinant protein research is their scalability. Using bacterial (e.g., *E. coli*), yeast, or mammalian cell systems, these proteins are mass-produced with high purity. This enables cost-effective manufacturing for pharmaceuticals (e.g., monoclonal antibodies, vaccines) or biocatalysts in biofuel production.
Clinically, TPS recombinant proteins have shown promise in treating cancers, autoimmune diseases, and infectious diseases. Their specificity reduces off-target effects compared to small-molecule drugs. However, challenges persist, including immunogenicity, production complexity, and ensuring proper post-translational modifications in non-native hosts.
Innovations like CRISPR-based editing and AI-driven protein design are accelerating TPS development. Future directions include multifunctional fusion proteins, personalized therapies, and sustainable biomanufacturing. As tools and knowledge expand, TPS recombinant proteins will remain pivotal in addressing global health and industrial challenges.
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*Note: TPS is context-dependent; adjust specifics based on the exact protein class referred to.*
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