| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FPB |
| Uniprot No | P51814 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-821aa |
| 氨基酸序列 | MAANGDSPPWSPALAAEGRGSSCEVRRERTPEARIHSVKRYPDLSPGPKGRSSADHAALNSIVSLQASVSFEDVTVDFSKEEWQHLDPAQRRLYWDVTLENYSHLLSVGYQIPKSEAAFKLEQGEGPWMLEGEAPHQSCSGEAIGKMQQQGIPGGIFFHCERFDQPIGEDSLCSILEELWQDNDQLEQRQENQNNLLSHVKVLIKERGYEHKNIEKIIHVTTKLVPSIKRLHNCDTILKHTLNSHNHNRNSATKNLGKIFGNGNNFPHSPSSTKNENAKTGANSCEHDHYEKHLSHKQAPTHHQKIHPEEKLYVCTECVMGFTQKSHLFEHQRIHAGEKSRECDKSNKVFPQKPQVDVHPSVYTGEKPYLCTQCGKVFTLKSNLITHQKIHTGQKPYKCSECGKAFFQRSDLFRHLRIHTGEKPYECSECGKGFSQNSDLSIHQKTHTGEKHYECNECGKAFTRKSALRMHQRIHTGEKPYVCADCGKAFIQKSHFNTHQRIHTGEKPYECSDCGKSFTKKSQLHVHQRIHTGEKPYICTECGKVFTHRTNLTTHQKTHTGEKPYMCAECGKAFTDQSNLIKHQKTHTGEKPYKCNGCGKAFIWKSRLKIHQKSHIGERHYECKDCGKAFIQKSTLSVHQRIHTGEKPYVCPECGKAFIQKSHFIAHHRIHTGEKPYECSDCGKCFTKKSQLRVHQKIHTGEKPNICAECGKAFTDRSNLITHQKIHTREKPYECGDCGKTFTWKSRLNIHQKSHTGERHYECSKCGKAFIQKATLSMHQIIHTGKKPYACTECQKAFTDRSNLIKHQKMHSGEKRYKASD |
| 预测分子量 | 93,7 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FPB重组蛋白的3篇参考文献示例，涵盖表达、功能及应用研究：
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1. **文献名称**：*Expression and Functional Characterization of Recombinant Fibrinopeptide B in Mammalian Cells*
**作者**：Smith J, et al.
**摘要**：本研究利用哺乳动物表达系统成功表达重组FPB蛋白，通过质谱与凝血实验证实其与天然FPB结构一致，并保留促进纤维蛋白交联的活性，为凝血机制研究提供新工具。
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2. **文献名称**：*Mutagenesis Analysis of Recombinant FPB Reveals Critical Residues for Thrombin Interaction*
**作者**：Chen L, Wang H.
**摘要**：通过定点突变技术筛选重组FPB中与凝血酶结合的关键氨基酸，发现Arg14和Gly19突变显著降低纤维蛋白原裂解效率，阐明FPB在凝血级联中的分子作用机制。
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3. **文献名称**：*Recombinant FPB Production in E. coli and Its Application in Thrombosis Models*
**作者**：Johnson R, et al.
**摘要**：报道利用大肠杆菌系统高效表达可溶性重组FPB，动物实验表明其可加速血栓形成，提示FPB作为促凝剂在止血治疗中的潜在应用价值。
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注：上述文献信息为模拟示例，实际研究中请通过PubMed、Web of Science等平台检索最新论文。
**Background of FPB Recombinant Protein**
FPB (Fibrinopeptide B) recombinant protein is a biologically engineered derivative of the natural FPB peptide, a critical component in the blood coagulation cascade. FPB originates from the proteolytic cleavage of fibrinogen by thrombin during clot formation. Specifically, thrombin cleaves fibrinogen’s Aα and Bβ chains, releasing fibrinopeptides A and B (FPA and FPB), respectively. This process exposes polymerization sites, enabling fibrin monomers to assemble into a stable fibrin clot.
Recombinant FPB is produced using genetic engineering techniques, where the gene encoding FPB is inserted into expression systems (e.g., *E. coli*, yeast, or mammalian cells) to achieve large-scale, high-purity production. This approach ensures consistency and avoids contaminants associated with plasma-derived proteins.
The study of recombinant FPB holds significance in both basic and applied research. Structurally, it aids in elucidating fibrinogen's role in hemostasis, thrombosis, and wound healing. Functionally, it serves as a biomarker for thrombin activity, helping diagnose coagulation disorders or monitor anticoagulant therapies. Additionally, recombinant FPB is utilized in developing biomaterials (e.g., fibrin-based scaffolds for tissue engineering) and therapeutic agents targeting clotting pathologies.
Recent advancements in protein engineering have further optimized FPB's stability and functional compatibility, expanding its applications in drug discovery and diagnostic assays. Its recombinant form also supports studies on fibrinogen mutations linked to bleeding or thrombotic diseases. Overall, FPB recombinant protein represents a vital tool in hematology research and clinical innovation, bridging insights into coagulation biology with therapeutic development.
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