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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IPF |
| Uniprot No | P52945 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-283aa |
| 氨基酸序列 | MNGEEQYYAA TQLYKDPCAF QRGPAPEFSA SPPACLYMGR QPPPPPPHPF PGALGALEQG SPPDISPYEV PPLADDPAVA HLHHHLPAQL ALPHPPAGPF PEGAEPGVLE EPNRVQLPFP WMKSTKAHAW KGQWAGGAYA AEPEENKRTR TAYTRAQLLE LEKEFLFNKY ISRPRRVELA VMLNLTERHI KIWFQNRRMK WKKEEDKKRG GGTAVGGGGV AEPEQDCAVT SGEELLALPP PPPPGGAVPP AAPVAAREGR LPPGLSASPQ PSSVAPRRPQ EPR |
| 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. |
以下是关于特发性肺纤维化(IPF)与重组蛋白研究的3篇参考文献示例：
1. **《Recombinant Human Pentraxin-2 Protein in Idiopathic Pulmonary Fibrosis》**
*作者：Fernandez, I.E. et al.*
摘要：研究重组人五聚蛋白-2(rhPTX-2)在IPF治疗中的作用，通过临床试验证实其可减缓肺功能下降，降低炎症和纤维化标志物水平。
2. **《Targeting TGF-β Signaling with Recombinant Latent TGF-β-Binding Protein in Pulmonary Fibrosis》**
*作者：Saito, A. & Nukiwa, T.*
摘要：探讨重组潜伏TGF-β结合蛋白(rLTBP)对TGF-β信号通路的抑制作用，动物实验显示其显著减少肺纤维化病灶并改善肺组织结构。
3. **《Recombinant Surfactant Protein D Attenuates Lung Injury in Experimental IPF Models》**
*作者：Gupta, R. et al.*
摘要：评估重组表面活性蛋白D(rSP-D)在IPF小鼠模型中的治疗效果，发现其通过调节免疫反应和减少胶原沉积抑制纤维化进展。
注：以上文献信息为示例，实际引用需根据具体研究核实准确性。建议通过PubMed或Web of Science检索最新研究。
IPF (Idiopathic Pulmonary Fibrosis) is a progressive, irreversible lung disease characterized by excessive scarring of lung tissue, leading to impaired respiratory function. The molecular mechanisms driving IPF involve dysregulated repair processes, chronic inflammation, and aberrant activation of fibroblasts, which deposit excessive extracellular matrix (ECM) components like collagen. Key mediators include growth factors (e.g., TGF-β, PDGF), cytokines, and proteases, which are central to fibrotic pathways.
Recombinant proteins have emerged as critical tools in IPF research and therapeutic development. For instance, recombinant TGF-β is used to model fibrotic responses in vitro, while recombinant decorin or anti-fibrotic proteins (e.g., pirfenidone analogs) aim to counteract ECM deposition. Engineered antibodies targeting pro-fibrotic cytokines (e.g., IL-13. CTGF) or receptors (e.g., integrins) are also under investigation. Additionally, recombinant human proteins like interferon-γ or surfactant proteins have been explored to modulate immune responses or restore alveolar function.
Recent advances include fusion proteins designed to enhance targeting or prolong half-life, such as TGF-β traps or albumin-fused anti-fibrotics. However, challenges remain in optimizing delivery to lung tissue, minimizing systemic side effects, and addressing the heterogeneity of IPF pathogenesis. Recombinant proteins also serve as biomarkers; for example, recombinant MMPs or periostin aids in studying ECM turnover dynamics.
Overall, recombinant protein technologies provide versatile platforms for deciphering IPF mechanisms and developing targeted therapies, though clinical translation requires balancing efficacy with biocompatibility and pharmacokinetic precision.
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