| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HMWK |
| Uniprot No | P01042 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 390-639aa |
| 氨基酸序列 | SSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDL |
| 预测分子量 | 31.8 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HMWK(高分子量激肽原)重组蛋白的虚构参考文献示例，内容基于常见研究方向模拟：
1. **《重组HMWK在大肠杆菌中的高效表达及功能验证》**
*作者：Chen L, et al.*
摘要：本研究通过优化密码子和表达条件，在大肠杆菌中成功表达可溶性HMWK重组蛋白，并验证其与血浆激肽释放酶的结合活性，为凝血相关药物开发提供基础。
2. **《HMWK结构域缺失突变体对炎症反应的调控机制》**
*作者：Wang Y, et al.*
摘要：利用哺乳动物细胞系统表达HMWK不同结构域缺失的重组蛋白，发现其结构域5在抑制缓激肽介导的血管通透性中起关键作用，揭示了HMWK抗炎功能的结构基础。
3. **《基于酵母系统的HMWK糖基化修饰及其对凝血功能的影响》**
*作者：Garcia R, et al.*
摘要：通过毕赤酵母表达糖基化修饰的HMWK重组蛋白，证明糖链修饰可增强其稳定性，并显著提高其在体外凝血模型中对接触激活通路的调控效率。
4. **《重组HMWK在遗传性血管性水肿动物模型中的治疗潜力》**
*作者：Tanaka K, et al.*
摘要：在小鼠模型中验证外源性重组HMWK蛋白可补偿C1抑制剂缺陷，降低缓激肽过度生成，缓解血管性水肿症状，提示其作为替代疗法的可能性。
注：以上内容为模拟文献，实际研究中建议通过学术数据库(如PubMed、Web of Science)以“HMWK recombinant protein”或“high molecular weight kininogen expression”为关键词检索最新成果。
HMWK (High Molecular Weight Kininogen) is a multifunctional plasma glycoprotein that plays a critical role in the intrinsic pathway of blood coagulation, inflammation, and the kallikrein-kinin system. As a key component of the contact activation system, it serves as a cofactor for the activation of factor XII (Hageman factor) and prekallikrein, ultimately leading to bradykinin release—a potent vasodilator and mediator of inflammatory responses. Structurally, HMWK consists of six domains (D1-D6) with distinct functional regions involved in binding to negatively charged surfaces, platelets, and endothelial cells.
Recombinant HMWK protein is engineered using biotechnological approaches to replicate the native protein's structure and function. This involves cloning the HMWK gene into expression vectors, followed by production in host systems such as bacterial, yeast, or mammalian cell cultures. Recombinant technology enables precise control over post-translational modifications critical for HMWK's biological activity, particularly glycosylation patterns in its heavy chain (D1-D3) and light chain (D5-D6).
The development of recombinant HMWK addresses challenges in studying and utilizing the native protein, which is difficult to isolate in pure form from plasma due to low abundance and complex interactions. It has become invaluable for research into coagulation disorders, vascular biology, and drug discovery—particularly for designing inhibitors targeting pathological bradykinin overproduction or contact system dysregulation. Additionally, recombinant HMWK serves as a standardized reagent in diagnostic assays and a potential therapeutic candidate for conditions involving kinin system imbalances. Its production underscores advancements in protein engineering to model complex plasma proteins for both basic science and clinical applications.
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