| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CFH |
| Uniprot No | P08603 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-449aa |
| 氨基酸序列 | EDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRCTLKPCDYPDIKHGGLYHENMRRPYFPVAVGKYYSYYCDEHFETPSGSYWDHIHCTQDGWSPAVPCLRKCYFPYLENGYNQNYGRKFVQGKSIDVACHPGYALPKAQTTVTCMENGWSPTPRCIRVKTCS |
| 预测分子量 | 50.5 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. |
1. **"Recombinant human complement factor H: functional analysis and therapeutic potential in age-related macular degeneration"**
*Authors: Schmidt CQ, et al.*
摘要：研究重组人补体因子H(CFH)的体外功能特性，验证其抑制补体激活的能力，为年龄相关性黄斑变性(AMD)的靶向治疗提供依据。
2. **"Production and characterization of recombinant human complement factor H in mammalian cell systems"**
*Authors: Sánchez-Corral P, et al.*
摘要：描述在哺乳动物细胞系统中高效表达重组人CFH的方法，证实其与天然CFH结构功能一致，可用于补体相关疾病的机制研究及药物开发。
3. **"Therapeutic targeting of complement factor H with recombinant protein CFHR1 in a mouse model of atypical hemolytic uremic syndrome"**
*Authors: Fakhouri F, et al.*
摘要：通过小鼠模型验证重组CFH类似物CFHR1对非典型溶血尿毒综合征(aHUS)的治疗效果，证明其可恢复补体调控平衡并减轻肾脏损伤。
4. **"Structural and functional characterization of a recombinant form of complement factor H: implications for therapy in C3 glomerulopathy"**
*Authors: Medjeral-Thomas NR, et al.*
摘要：解析重组CFH蛋白的结构与功能，探索其在C3肾小球病中恢复补体稳态的潜力，为临床前研究提供数据支持。
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以上文献聚焦于重组CFH的生产、功能验证及在补体相关疾病(如AMD、aHUS、C3肾小球病)中的治疗应用，涵盖基础研究与转化医学方向。
**Background of Recombinant CFH Protein**
Complement Factor H (CFH) is a critical regulatory protein in the innate immune system, primarily responsible for controlling the alternative pathway (AP) of the complement system. This glycoprotein, composed of 20 short consensus repeat (SCR) domains, acts as a soluble inhibitor to prevent excessive complement activation on host cells and tissues. By binding to C3b, glycosaminoglycans, and other surface markers, CFH accelerates the decay of the C3 convertase (C3bBb) and serves as a cofactor for factor I-mediated cleavage of C3b, thus protecting healthy cells from complement-mediated damage.
Dysregulation or genetic mutations in CFH are strongly linked to several diseases, including atypical hemolytic uremic syndrome (aHUS), age-related macular degeneration (AMD), and C3 glomerulopathies (C3G). These conditions arise from uncontrolled AP activation, leading to inflammation, tissue injury, and organ dysfunction. For instance, CFH mutations impair its binding to host surfaces, rendering cells vulnerable to complement attack.
Recombinant CFH (rCFH) is produced via biotechnological methods, often using mammalian expression systems (e.g., CHO cells) to ensure proper post-translational modifications. It retains the functional domains necessary for complement regulation and has emerged as a therapeutic candidate. In preclinical and clinical studies, rCFH has shown potential in restoring complement homeostasis in CFH-deficient or dysfunctional states. For example, it may supplement endogenous CFH in genetic disorders or block pathological complement activation in autoimmune diseases.
Research also explores engineered CFH variants, such as mini-CFH (containing key SCR domains), to enhance tissue targeting or bioavailability. Despite challenges in production costs and immunogenicity, rCFH represents a promising strategy for precision therapies in complement-driven diseases, bridging gaps in understanding disease mechanisms and treatment development. Its application extends to diagnostic tools and drug screening platforms, underscoring its multifaceted role in biomedical innovation.
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