| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ideS |
| Uniprot No | F8V4V0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-341aa |
| 氨基酸序列 | DSFSANQEIRYSEVTPYHVTSVWTKGVTPPAKFTQGEDVFHAPYVANQGWYDITKTFNGKDDLLCGAATAGNMLHWWFDQNKEKIEAYLKKHPDKQKIMFGDQELLDVRKVINTKGDQTNSELFNYFRDKAFPGLSARRIGVMPDLVLDMFINGYYLNVYKTQTTDVNRTYQEKDRRGGIFDAVFTRGDQSKLLTSRHDFKEKNLKEISDLIKKELTEGKALGLSHTYANVRINHVINLWGADFDSNGNLKAIYVTDSDSNASIGMKKYFVGVNSAGKVAISAKEIKEDNIGAQVLGLFTLSTGQDSWNQTN |
| 预测分子量 | 36.9 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ideS重组蛋白的3-4篇参考文献及其简要摘要：
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1. **文献名称**：*"IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G"*
**作者**：von Pawel-Rammingen U, Johansson BP, Björck L
**摘要**：该研究首次从化脓性链球菌中鉴定并克隆了ideS酶，证明其是一种半胱氨酸蛋白酶，能特异性地水解人IgG的铰链区，破坏抗体功能，为后续治疗应用奠定基础。
2. **文献名称**：*"A therapeutic streptococcal enzyme for acute antibody-mediated transplant rejection: IdeS cleaves donor-specific alloantibodies"*
**作者**：Ryan MHY, et al.
**摘要**：研究评估了重组ideS在移植排斥中的潜力，发现其能快速裂解供体特异性IgG抗体，缓解抗体介导的急性排斥反应，为器官移植提供新疗法。
3. **文献名称**：*"Structural basis for the substrate specificity of the immunoglobulin G-degrading enzyme IdeS"*
**作者**：Leung K, et al.
**摘要**：通过X射线晶体学解析ideS的三维结构，揭示了其与IgG结合的分子机制，解释了其对IgG铰链区的高度特异性。
4. **文献名称**：*"IgG Endopeptidase in Highly Sensitized Patients Undergoing Transplantation"*
**作者**：Jordan SC, et al.
**摘要**：临床试验表明，重组ideS(商品名Imlifidase)能快速降解IgG抗体，使高致敏患者成功接受肾移植，验证了其临床安全性和有效性。
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这些文献涵盖了ideS的发现、机制研究及临床应用，反映了其在生物医学领域的潜力。
IdeS, the Immunoglobulin G (IgG)-degrading enzyme of *Streptococcus pyogenes*, is a highly specific bacterial protease that cleaves human IgG antibodies at the hinge region, disrupting their effector functions. Originally identified as a virulence factor in *S. pyogenes*—a pathogenic bacterium causing infections ranging from pharyngitis to necrotizing fasciitis—IdeS enables immune evasion by degrading IgG, a critical component of humoral immunity. This 34-kDa cysteine protease exhibits remarkable substrate specificity, targeting the heavy chain of IgG with no activity against other immunoglobulin classes or structurally related proteins.
The recombinant form of IdeS (rIdeS) is produced via genetic engineering in heterologous expression systems like *E. coli* or mammalian cell lines. This recombinant protein retains the enzymatic properties of native IdeS, making it a valuable tool for research and therapeutic applications. Its ability to rapidly cleave IgG has attracted interest in clinical settings, particularly for mitigating antibody-mediated pathologies. For example, rIdeS has been explored in autoimmune diseases and transplant rejection, where IgG antibodies drive tissue damage. In 2020. rIdeS (imlifidase) received conditional approval in the EU and the USA for desensitization in kidney transplantation, demonstrating its potential to neutralize donor-specific antibodies pre-transplant.
Beyond therapeutics, rIdeS serves as a biochemical tool for studying IgG structure-function relationships, antibody-drug conjugate analysis, and Fc-mediated immune responses. Its mechanism—hydrolyzing a single peptide bond in IgG’s hinge—also offers insights into bacterial pathogenesis and host-pathogen interactions. Recent structural studies have further elucidated its catalytic domain and substrate-binding motifs, guiding engineering efforts to optimize stability and activity. As a targeted IgG-cleaving agent, recombinant IdeS bridges microbiology, immunology, and biotechnology, highlighting its dual role as both a bacterial weapon and a biomedical resource.
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