| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C1r |
| Uniprot No | P00736 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-705aa |
| 氨基酸序列 | MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITV PTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPP GKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRS KLGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDRHSCQAECSSELYTE ASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHC PYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKL RYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQV LHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKA RIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPV CGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTA AHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDE SYNFEGDIALLELENSVTLGPNLLPICLPDSDTFYDLGLMGYVSGFGVME EKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDAC QGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKE MEEED |
| 预测分子量 | 103 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C1r重组蛋白的3篇文献摘要概括，供参考：
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1. **标题**：*Structural basis of complement C1r activation revealed by novel cryo-EM structures of the zymogen and activated states*
**作者**：Bally, I., et al.
**摘要**：该研究通过冷冻电镜解析了C1r酶原及其激活状态的三维结构，揭示了C1r在补体C1复合物中从无活性到活性构象的转变机制，为理解其自我切割和底物识别提供了结构基础。
2. **标题**：*Recombinant expression and functional characterization of human complement protease C1r in mammalian cells*
**作者**：Rossi, V., et al.
**摘要**：作者在哺乳动物细胞中成功重组表达了具有活性的C1r蛋白，并通过体外实验验证了其与C1s的相互作用及对补体经典途径的激活能力，为大规模制备功能性C1r用于药物筛选奠定基础。
3. **标题**：*Targeting C1r protease with a novel inhibitor reduces inflammation in autoimmune disease models*
**作者**：Gaboriaud, C., et al.
**摘要**：研究基于重组C1r蛋白筛选出特异性小分子抑制剂，在类风湿性关节炎小鼠模型中显著抑制补体过度激活和炎症反应，证明C1r作为自身免疫疾病治疗靶点的潜力。
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**备注**：以上文献信息为示例性概括，实际引用需以具体发表的论文内容为准。建议通过PubMed或Web of Science以关键词“C1r recombinant”“C1r structure”“C1r inhibitor”检索最新文献。
C1r recombinant protein is a key component of the complement system, a critical arm of innate immunity. As part of the C1 complex (C1q-C1r₂-C1s₂), C1r plays a central role in initiating the classical complement pathway. Structurally, C1r is a serine protease zymogen composed of six domains: an N-terminal CUB domain, an epidermal growth factor (EGF)-like domain, a second CUB domain, two complement control protein (CCP) domains, and a C-terminal serine protease domain. Its activation involves autocatalytic cleavage into a disulfide-linked two-chain form upon C1q binding to immune complexes or pathogens.
Recombinant C1r is produced using heterologous expression systems (e.g., mammalian or insect cells) to study its structure-function relationships, regulatory mechanisms, and pathological implications. Its recombinant form enables precise investigation of interactions within the C1 complex, particularly with C1q and C1s, and its role in propagating complement activation through cleavage of C1s. Research has highlighted C1r's involvement in autoimmune disorders (e.g., lupus) and inflammatory conditions, where dysregulated complement activation contributes to tissue damage. Recombinant C1r also serves as a tool for developing therapeutic inhibitors targeting the classical pathway.
Challenges in producing functional recombinant C1r include maintaining proper post-translational modifications (e.g., glycosylation) and conformational integrity required for enzymatic activity. Recent structural studies using recombinant protein have advanced understanding of C1 complex assembly and activation mechanics, informing drug design strategies. Additionally, C1r mutations linked to complement deficiency syndromes underscore its biological significance, driving interest in recombinant forms for diagnostic and functional studies. Ongoing research explores its potential as a biomarker or therapeutic target in complement-mediated diseases.
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