纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | C1S |
Uniprot No | P09871 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-688aa |
氨基酸序列 | MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED |
预测分子量 | 76,6 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C1S重组蛋白的3篇模拟参考文献示例(注:部分文献信息为示例性概括,非真实存在):
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1. **标题**:*Expression and Functional Characterization of Recombinant Human C1s Protease in HEK293 Cells*
**作者**:Smith J, et al.
**摘要**:本研究利用哺乳动物HEK293细胞成功表达重组人C1s蛋白,并验证其酶活性。通过免疫沉淀纯化后,证实重组C1s可有效切割补体C4和C2.为研究补体经典通路提供工具。
2. **标题**:*Structural Insights into the Zymogen Activation of C1s in the Complement System*
**作者**:Zhang L, et al.
**摘要**:通过X射线晶体学解析重组C1s酶原及其激活形式的空间结构,揭示其自抑制机制及底物结合位点特征,为开发补体相关疾病的抑制剂奠定基础。
3. **标题**:*Optimization of Recombinant C1s Production in E. coli for Antibody Degradation Studies*
**作者**:Lee H, et al.
**摘要**:优化大肠杆菌表达系统提高重组C1s产量,通过包涵体复性获得高纯度蛋白,并证明其可特异性切割IgG抗体,用于体外免疫复合物清除研究。
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**备注**:以上文献为模拟概括,实际研究中建议通过PubMed、Google Scholar等平台以“recombinant C1s protein”、“C1s protease expression”等关键词检索最新文献。
**Background of C1S Recombinant Protein**
C1S, a serine protease component of the C1 complex within the complement system, plays a critical role in the classical pathway of complement activation. This pathway is essential for innate immunity, targeting pathogens and damaged cells for clearance. C1S is synthesized as a zymogen and becomes activated when the C1 complex binds to immune complexes (e.g., antigen-antibody complexes). Activated C1S cleaves complement proteins C4 and C2. initiating the formation of the C3 convertase, a central enzyme in complement-mediated inflammatory and lytic responses.
Dysregulation of C1S is linked to autoimmune diseases (e.g., systemic lupus erythematosus), inflammatory disorders, and age-related macular degeneration. These associations have driven interest in developing therapeutic inhibitors targeting C1S. Recombinant C1S protein, produced via genetic engineering in mammalian expression systems (e.g., CHO or HEK293 cells), retains native structure and enzymatic activity. Its production enables detailed biochemical studies, drug screening, and structural analyses (e.g., crystallography) to elucidate mechanisms of complement activation and inhibition.
Therapeutically, recombinant C1S is used to validate inhibitors, such as monoclonal antibodies or small molecules, in preclinical models. Notably, C1S-targeting drugs are in clinical trials for complement-mediated diseases. Additionally, recombinant C1S serves as a tool to study autoimmune conditions, where excessive complement activation contributes to tissue damage. Beyond therapeutics, it aids in diagnostic assays for monitoring complement activity in patient samples.
In summary, recombinant C1S bridges basic research and clinical applications, offering insights into complement biology and paving the way for novel treatments targeting immune dysregulation.
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