| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAP |
| Uniprot No | Q12884 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-760aa |
| 氨基酸序列 | LRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD |
| 预测分子量 | 86.5 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篇关于FAP(Fibroblast Activation Protein)重组蛋白的示例文献(内容为虚构示例，实际文献请通过学术数据库查询)：
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1. **文献名称**: "Structural Insights into Fibroblast Activation Protein Alpha and Its Role in Tumor Microenvironment"
**作者**: Smith J, et al.
**摘要**: 通过X射线晶体学解析了人源FAPα重组蛋白的催化结构域结构，揭示了其底物结合位点的构象变化，并探讨其在肿瘤基质重塑中的功能机制。
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2. **文献名称**: "Recombinant FAP Protein as a Therapeutic Target in Pancreatic Cancer"
**作者**: Li X, Wang Y.
**摘要**: 研究利用重组FAP蛋白开发特异性抗体，验证其在胰腺癌小鼠模型中抑制肿瘤生长和转移的效果，证明靶向FAP可增强化疗敏感性。
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3. **文献名称**: "Expression and Purification of Active Recombinant FAP in E. coli for Enzymatic Characterization"
**作者**: Gonzalez R, et al.
**摘要**: 报道了一种在大肠杆菌中高效表达可溶性FAP重组蛋白的方法，通过优化诱导条件获得高活性酶，并分析其体外切割胶原蛋白的动力学参数。
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4. **文献名称**: "FAP-Dependent Extracellular Matrix Remodeling in Fibrotic Diseases"
**作者**: Chen L, et al.
**摘要**: 利用重组FAP蛋白研究其在肺纤维化模型中的酶活性调控，发现FAP通过降解特定ECM成分促进成纤维细胞活化，提示其作为抗纤维化靶点的潜力。
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**注意**：以上文献信息为模拟示例，实际研究中请通过PubMed、Web of Science或Google Scholar等平台检索真实文献。
**Background of FAP Recombinant Protein**
Fibroblast activation protein (FAP) is a type II transmembrane glycoprotein belonging to the serine protease family, characterized by dual enzymatic activities: dipeptidyl peptidase and endopeptidase. It is predominantly expressed on activated fibroblasts in pathological conditions, including solid tumors, fibrotic tissues, and sites of chronic inflammation. In healthy tissues, FAP expression is minimal, making it a compelling target for therapeutic and diagnostic applications.
FAP gained attention due to its role in remodeling the extracellular matrix (ECM) and modulating cell signaling pathways. In cancer, FAP-positive fibroblasts (often termed cancer-associated fibroblasts, CAFs) contribute to tumor progression by promoting angiogenesis, immune evasion, and metastasis. Similarly, in fibrosis, FAP overexpression correlates with excessive ECM deposition and tissue stiffening. These pathological roles have spurred interest in developing FAP-targeted therapies, such as inhibitors, antibodies, and immunotherapies.
Recombinant FAP protein, produced via genetic engineering in systems like mammalian cells or *E. coli*, retains the enzymatic and structural features of native FAP. It serves as a critical tool for studying FAP’s biological functions, screening inhibitors, and engineering targeted therapies. For instance, FAP recombinant proteins are used in structural studies to map substrate-binding sites or design selective inhibitors. They also underpin the development of FAP-targeted imaging probes (e.g., PET tracers) for non-invasive detection of tumors or fibrotic lesions.
Recent research highlights FAP’s potential as a theranostic target. Clinical trials exploring FAP-directed CAR-T cells, antibody-drug conjugates, or small-molecule inhibitors underscore its translational relevance. However, challenges remain, including understanding FAP’s context-dependent roles and minimizing off-target effects. The availability of high-purity, bioactive FAP recombinant protein continues to accelerate both mechanistic studies and therapeutic innovation, positioning FAP as a pivotal molecule in precision medicine for cancer and fibrosis.
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