| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AT |
| Uniprot No | Q4VNC1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1196aa |
| 氨基酸序列 | MGHFEKGQHALLNEGEENEMEIFGYRTQGCRKSLCLAGSIFSFGILPLVFYWRPAWHVWAHCVPCSLQEADTVLLRTTDEFQIYSWKKVIWIYLSALNSAFGLTPDHPLMTDEEYIINRAIRKPDLKVRCIKVQKIRYVWNYLEGQFQKIGSLEDWLSSAKIHQKFGSGLTREEQEIRRLICGPNTIDVEVTPIWKLLIKEVLNPFYIFQLFSVCLWFSEDYKEYAFAIIIMSIISISLTVYDLREQSVKLHHLVESHNSITVSVCGRKAGVQELESRVLVPGDLLILTGNKVLMPCDAVLIEGSCVVDEGMLTGESIPVTKTPLPKMDSSVPWKTQSEADYKRHVLFCGTEVIQAKAACSGTVRAVVLQTGFNTAKGDLVRSILYPKPVNFQLYRDAIRFLLCLVGTATIGMIYTLCVYVLSGEPPEEVVRKALDVITIAVPPALPAALTTGIIYAQRRLKKRGIFCISPQRINVCGQLNLVCFDKTGTLTRDGLDLWGVVSCDRNGFQEVHSFASGQALPWGPLCAAMASCHSLILLDGTIQGDPLDLKMFEATTWEMAFSGDDFHIKGVPAHAMVVKPCRTASQVPVEGIAILHQFPFSSALQRMTVIVQEMGGDRLAFMKGAPERVASFCQPETVPTSFVSELQIYTTQGFRVIALAYKKLENDHHATTLTRETVESDLIFLGLLILENRLKEETKPVLEELISARIRTVMITGDNLQTAITVARKSGMVSESQKVILIEANETTGSSSASISWTLVEEKKHIMYGNQDNYINIRDEVSDKGREGSYHFALTGKSFHVISQHFSSLLPKILINGTIFARMSPGQKSSLVEEFQKLDYFVGMCGDGANDCGALKMAHVGISLSEQEASVASPFTSKTPNIECVPHLIKEGRAALVTSFCMFKYMALYSMIQYVGVLLLYWETNSLSNYQFLFQDLAITTLIGVTMNLNGAYPKLVPFRPAGRLISPPLLLSVIFNILLSLAMHIAGFILVQRQPWYSVEIHSACTVQNESISELTMSPTAPEKMESNSTFTSFENTTVWFLGTINCITVALVFSKGKPFRQPTYTNYIFVLVLIIQLGVCLFILFADIPELYRRLDLLCTPVLWRASIVIMLSLNFIVSLVAEEAVIENRALWMMIKRCFGYQSKSQYRIWQRDLANDPSWPPLNQTSHSDMPECGRGVSYSNPVFESNEEQL |
| 预测分子量 | 133,9 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. |
以下是关于重组抗凝血酶(AT)蛋白的3篇代表性文献示例(部分信息为虚构，仅供格式参考)：
1. **文献名称**：Recombinant Antithrombin Production in Escherichia coli: Optimization and Functional Characterization
**作者**：Johnson, R. et al.
**摘要**：本研究通过优化大肠杆菌表达系统，成功实现了重组人抗凝血酶的高效可溶性表达。通过体外活性测定，证实其具有与血浆来源AT相似的肝素结合能力和凝血酶抑制活性。
2. **文献名称**：Structural Analysis of Glycosylated Recombinant Antithrombin III Expressed in CHO Cells
**作者**：Smith, L. et al.
**摘要**：利用CHO细胞表达系统制备糖基化重组AT-III，通过X射线晶体学解析其三维结构，揭示了N-连接糖链对蛋白构象稳定性和抗凝血功能的关键作用，为治疗用重组AT的质量控制提供结构基础。
3. **文献名称**：Phase III Clinical Trial of Recombinant Antithrombin for Hereditary Deficiency Therapy
**作者**：Anderson, C. et al.
**摘要**：针对遗传性AT缺乏症患者的多中心临床试验显示，每周静脉注射重组AT可有效维持血浆AT活性>80%，显著降低静脉血栓发生率(p<0.01)，且未发现严重不良反应。
注：实际文献检索建议使用关键词"recombinant antithrombin"或"recombinant AT III"在PubMed/Web of Science等数据库查询。真实研究多集中于表达系统优化(如哺乳动物细胞系改造)、糖基化修饰对药效的影响，以及其在脓毒症、DIC等危重症中的应用评估。
**Background of Recombinant Antithrombin (AT)**
Antithrombin (AT), a key serine protease inhibitor in the hemostatic system, plays a critical role in regulating blood coagulation by neutralizing thrombin, factor Xa, and other clotting enzymes. Naturally synthesized in the liver, AT’s activity is significantly enhanced by heparin, a mechanism vital for preventing excessive clot formation. Hereditary or acquired AT deficiency, though rare, increases thrombosis risk, necessitating therapeutic intervention.
Traditional AT replacement therapies relied on plasma-derived concentrates, which carry potential risks of pathogen transmission and limited supply. Recombinant AT (rAT), produced via genetic engineering in mammalian cell cultures (e.g., CHO cells), emerged as a safer, scalable alternative. The recombinant form mirrors the native protein’s structure and function, including glycosylation patterns essential for stability and heparin-binding affinity.
Approved for clinical use in congenital AT deficiency, rAT is administered to prevent thromboembolic events during high-risk situations like surgery or childbirth. Beyond hereditary cases, it is explored in acquired conditions such as sepsis-induced disseminated intravascular coagulation (DIC) or heparin resistance during cardiac surgeries. Its consistent purity and reduced immunogenicity make it preferable over plasma-derived counterparts.
Research also investigates rAT’s anti-inflammatory and cytoprotective properties, potentially broadening its therapeutic scope. However, challenges like high production costs and the need for frequent dosing due to its short half-life persist. Innovations in protein engineering, such as PEGylation or fusion technologies, aim to enhance pharmacokinetics and efficacy.
Overall, recombinant AT exemplifies the convergence of biotechnology and hematology, offering targeted therapy for coagulation disorders while underscoring the importance of optimizing biologics for clinical and economic viability.
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