| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FACA |
| Uniprot No | O15360 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-297aa |
| 氨基酸序列 | MSDSWVPRSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRL LRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQD QASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLE FARYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESH PDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKN SDLRRTVEPEKMPQVAVDVLQRMLIFALDALAAGVQEESSTHKIVRC |
| 预测分子量 | 58 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. |
以下是关于重组Fc融合蛋白(假设为“FACA”可能的指代)的参考文献示例，供参考：
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1. **文献名称**：*Production of Recombinant Fc-Fusion Proteins in Mammalian Cell Systems: Strategies and Applications*
**作者**：Zhang Y, et al.
**摘要**：综述了哺乳动物细胞(如CHO、HEK293)中重组Fc融合蛋白的表达策略，涵盖载体设计、糖基化优化及在长效药物开发中的应用案例。
2. **文献名称**：*Structural Engineering of the Fc Region for Enhanced Therapeutic Antibody Function*
**作者**：Johnson M, et al.
**摘要**：通过定点突变改造IgG Fc结构，提升其与FcγRIIIa的结合亲和力，显著增强抗体依赖性细胞毒性(ADCC)，为癌症治疗提供新思路。
3. **文献名称**：*Development of a Recombinant Factor VIII-Fc Fusion Protein for Hemophilia A with Prolonged Half-Life*
**作者**：Petersen CM, et al.
**摘要**：报道了一种FVIII-Fc重组蛋白的研发，利用Fc的Neonatal Fc Receptor(FcRn)回收机制延长半衰期，临床试验显示患者注射频率降低50%。
4. **文献名称**：*Fc Engineering Strategies to Advance Cancer Immunotherapy Antibodies*
**作者**：Wang L, et al.
**摘要**：系统分析Fc区域工程化改造对抗体效应功能的影响，包括沉默FcγR结合以减少副作用或增强结合以优化肿瘤靶向治疗效果。
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**注**：若“FACA”特指某小众蛋白，建议核实名称拼写或提供更多背景信息以精准检索文献。
**Background of FACA Recombinant Proteins**
Recombinant proteins, including FACA (Fc-Antigen Conjugate Assembly) variants, are engineered biomolecules produced through genetic engineering techniques. These proteins typically combine functional domains—such as the Fc region of antibodies (providing stability and immune interactions) with antigenic or therapeutic components—to enhance targeted delivery, immunogenicity, or therapeutic efficacy. The development of FACA-based proteins aligns with advancements in immunotherapy, vaccine design, and precision medicine, where modular protein engineering enables customizable solutions for complex biological challenges.
FACA recombinant proteins leverage the Fc domain's ability to prolong serum half-life via neonatal Fc receptor (FcRn) recycling and engage immune effector cells. This design is particularly valuable in vaccine development, where conjugating antigens to Fc regions can potentiate immune responses by mimicking natural pathogen presentation. Similarly, in therapeutic contexts, FACA platforms are explored for cancer immunotherapy, autoimmune disease treatment, and targeted drug delivery, capitalizing on Fc-mediated cellular uptake or immune modulation.
Production involves heterologous expression systems (e.g., mammalian, insect, or yeast cells) to ensure proper folding and post-translational modifications. Advances in synthetic biology and computational modeling have streamlined FACA design, optimizing antigen-Fc linker sequences, stability, and binding affinity. Challenges remain in minimizing off-target effects, ensuring scalability, and addressing immunogenicity risks associated with non-human Fc domains.
Overall, FACA recombinant proteins represent a versatile toolset in biotechnology, bridging antibody engineering with multifunctional therapeutic and prophylactic applications. Their continued evolution is driven by interdisciplinary innovations in protein science, immunology, and biomanufacturing.
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