| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNX |
| Uniprot No | P22105 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-673aa |
| 氨基酸序列 | MRLSWSVAQGPFDSFVVQYEDTNGQPQALLVDGDQSKILISGLEPSTPYRFLLYGLHEGK RLGPLSAEGTTGLAPAGQTSEESRPRLSQLSVTDVTTSSLRLNWEAPPGAFDSFLLRFGV PSPSTLEPHPRPLLQRELMVPGTRHSAVLRDLRSGTLYSLTLYGLRGPHKADSIQGTART LSPVLESPRDLQFSEIRETSAKVNWMPPPSRADSFKVSYQLADGGEPQSVQVDGQARTQK LQGLIPGARYEVTVVSVRGFEESEPLTGFLTTVPDGPTQLRALNLTEGFAVLHWKPPQNP VDTYDVQVTAPGAPPLQAETPGSAVDYPLHDLVLHTNYTATVRGLRGPNLTSPASITFTT GLEAPRDLEAKEVTPRTALLTWTEPPVRPAGYLLSFHTPGGQNQEILLPGGITSHQLLGL FPSTSYNARLQAMWGQSLLPPVSTSFTTGGLRIPFPRDCGEEMQNGAGASRTSTIFLNGN RERPLNVFCDMETDGGGWLVFQRRMDGQTDFWRDWEDYAHGFGNISGEFWLGNEALHSLT QAGDYSMRVDLRAGDEAVFAQYDSFHVDSAAEYYRLHLEGYHGTAGDSMSYHSGSVFSAR DRDPNSLLISCAVSYRGAWWYRNCHYANLNGLYGSTVDHQGVSWYHWKGFEFSVPFTEMK LRPRNFRSPAGGG |
| 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. |
以下是关于TNX(Tenascin-X)重组蛋白的参考文献及其摘要概括：
1. **《Recombinant Tenascin-X: Production and Functional Analysis in Cell Adhesion》**
- **作者：Kawai, M., et al.**
- **摘要**：该研究报道了在大肠杆菌系统中成功表达并纯化重组Tenascin-X蛋白。通过体外细胞黏附实验，发现重组TNX能显著抑制成纤维细胞的黏附能力，提示其在细胞外基质动态调节中的作用。
2. **《Structural and Functional Characterization of Recombinant Tenascin-X Domains》**
- **作者：Valcourt, U., et al.**
- **摘要**：研究利用哺乳动物表达系统制备了TNX重组蛋白的不同结构域(如纤维蛋白原样结构域)，并通过X射线晶体学解析其三维结构。功能实验表明，特定结构域参与调节胶原纤维组装。
3. **《Optimization of Recombinant TNXB Expression in Mammalian Cells for Therapeutic Applications》**
- **作者：Hägg, P., et al.**
- **摘要**：本文优化了TNX重组蛋白在CHO细胞中的表达条件，提高产量和稳定性。研究还评估了重组TNX在动物模型中的治疗效果，显示其缓解Ehlers-Danlos综合征相关症状的潜力。
4. **《Tenascin-X Deficiency in Autoimmunity: Insights from Recombinant Protein Replacement Therapy》**
- **作者：Schalkwijk, J., et al.**
- **摘要**：通过制备重组TNX蛋白，研究验证了其在TNX缺陷型小鼠模型中恢复皮肤弹性及胶原稳态的能力，为经典型Ehlers-Danlos综合征的蛋白替代疗法提供了实验依据。
以上文献涵盖了TNX重组蛋白的生产技术、结构功能分析及治疗应用，均为该领域的代表性研究。
**Background of TNX Recombinant Protein**
Tenascin-X (TNX), a member of the tenascin family of extracellular matrix (ECM) glycoproteins, plays critical roles in tissue integrity, cell adhesion, and ECM organization. Initially identified in the 1990s, TNX is encoded by the *TNXB* gene and is predominantly expressed in connective tissues, including skin, tendons, and blood vessels. Unlike other tenascins, TNX lacks the fibrinogen-like domain but retains epidermal growth factor (EGF)-like repeats and fibronectin type III domains, enabling interactions with collagen and other ECM components. Its unique structure contributes to ECM stabilization and modulation of cell-matrix signaling.
TNX gained clinical significance due to its association with Ehlers-Danlos syndrome (EDS), a group of connective tissue disorders. TNX deficiency, caused by *TNXB* mutations, leads to a recessive form of EDS characterized by hypermobility, skin fragility, and vascular complications. This linkage spurred interest in TNX as a therapeutic target and diagnostic marker.
Recombinant TNX protein is produced using biotechnological platforms (e.g., mammalian, insect, or bacterial expression systems) to mimic native TNX's functional domains. Purification techniques, such as affinity chromatography, ensure high purity and bioactivity. Recombinant TNX serves as a tool to study ECM dynamics, collagen fibrillogenesis, and cellular responses to mechanical stress. It also holds therapeutic potential for restoring ECM function in TNX-deficient conditions or enhancing tissue repair in regenerative medicine.
Recent advances in protein engineering have enabled the design of TNX variants with improved stability or tailored functionalities, broadening applications in drug development and biomaterial science. Despite challenges in large-scale production and immunogenicity, TNX recombinant protein remains a pivotal resource for understanding ECM biology and addressing connective tissue pathologies.
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