| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KLK11 |
| Uniprot No | Q9UBX7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-250aa |
| 氨基酸序列 | IIKGFECKPHSQPWQAALFEKTRLLCGATLIAPRWLLTAAHCLKPRYIVH LGQHNLQKEE GCEQTRTATESFPHPGFNNSLPNKDHRNDIMLVKMASPVSITWAVRPLTL SSRCVTAGTS CLISGWGSTSSPQLRLPHTLRCANITIIEHQKCENAYPGNITDTMVCASV QEGGKDSCQG DSGGPLVCNQSLQGIISWGQDPCAITRKPGVYTKVCKYVDWIQETMKNNV DHHHHHH |
| 预测分子量 | 25 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KLK11重组蛋白的3篇参考文献示例(文献信息为模拟生成，非真实文献)：
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1. **标题**: *Expression and characterization of recombinant human kallikrein 11 in mammalian cells*
**作者**: Smith A, et al.
**摘要**: 研究通过哺乳动物细胞表达系统(如HEK293)成功制备重组人KLK11蛋白，分析了其酶活性及底物特异性，发现其对特定肽链具有选择性切割能力，为后续功能研究奠定基础。
2. **标题**: *KLK11 recombinant protein as a potential biomarker in ovarian cancer*
**作者**: Lee B, et al.
**摘要**: 通过大肠杆菌表达纯化重组KLK11蛋白，发现其在卵巢癌患者血清中显著高表达。实验表明重组KLK11可用于开发诊断试剂，并可能参与肿瘤微环境调控。
3. **标题**: *Structural insights into KLK11 activation by recombinant protein crystallography*
**作者**: Chen X, et al.
**摘要**: 利用重组KLK11蛋白进行X射线晶体学研究，解析其三维结构及激活机制，发现特定离子结合位点对其酶活性的关键影响，为设计靶向抑制剂提供结构基础。
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注：以上内容为示例，实际文献需通过PubMed或Web of Science等平台检索关键词(如"recombinant KLK11")获取。如需真实文献，建议查阅相关数据库。
Kallikrein-related peptidase 11 (KLK11) is a serine protease encoded by the KLK11 gene, part of the human tissue kallikrein gene family located on chromosome 19q13.4. This family comprises 15 conserved serine proteases involved in diverse physiological processes, including hormone processing, skin desquamation, and inflammation. KLK11 is primarily expressed in hormone-regulated tissues (e.g., prostate, breast, ovary) and bodily fluids like seminal plasma and cerebrospinal fluid. It functions through proteolytic cleavage of substrates such as kininogens, extracellular matrix components, and other kallikreins, playing roles in tissue remodeling, cell signaling, and carcinogenesis.
Recombinant KLK11 refers to the engineered form of this protein produced in heterologous expression systems (e.g., Escherichia coli, mammalian cells) for research and therapeutic applications. Its production enables controlled study of KLK11's biochemical properties, substrate specificity, and regulatory mechanisms. Notably, KLK11 shows clinical relevance in cancer, with altered expression observed in prostate, ovarian, and breast cancers. Downregulation of KLK11 is linked to tumor progression and poor prognosis, suggesting potential as a diagnostic biomarker or therapeutic target.
Recombinant KLK11 is utilized to investigate its tumor-suppressive roles, including induction of apoptosis and inhibition of angiogenesis. Structural studies of the recombinant protein have identified critical residues for enzymatic activity and glycosylation patterns influencing stability. Challenges in production include maintaining proper post-translational modifications, often addressed using mammalian expression systems. Current research focuses on understanding its interaction networks and developing KLK11-based assays for early cancer detection. Its recombinant form remains vital for deciphering pathophysiological roles and translational applications in precision medicine.
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