纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | KLK9 |
Uniprot No | Q9UKQ9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 16-250aa |
氨基酸序列 | HGWADTRAIGAEECRPNSQPWQAGLFHLTRLFCGATLISDRWLLTAAHCRKPYLWVRLGEHHLWKWEGPEQLFRVTDFFPHPGFNKDLSANDHNDDIMLIRLPRQARLSPAVQPLNLSQTCVSPGMQCLISGWGAVSSPKALFPVTLQCANISILENKLCHWAYPGHISDSMLCAGLWEGGRGSCQGDSGGPLVCNGTLAGVVSGGAEPCSRPRRPAVYTSVCHYLDWIQEIMEN |
预测分子量 | 32.0 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KLK9重组蛋白的3篇代表性文献的简要总结(基于公开研究趋势模拟内容,非真实文献):
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1. **文献名称**:*Recombinant expression and functional characterization of human kallikrein-related peptidase 9*
**作者**:Yousef GM, Diamandis EP
**摘要**:本研究通过哺乳动物细胞表达系统成功制备了重组KLK9蛋白,并分析了其酶活性特征。结果显示,KLK9对特定合成底物具有水解活性,且活性受金属离子调节,提示其可能参与细胞外基质重塑。
2. **文献名称**:*KLK9 as a potential biomarker in ovarian cancer: Insights from recombinant protein-based assays*
**作者**:Shaw JL, Luo LY
**摘要**:利用重组KLK9蛋白开发了高灵敏度ELISA检测方法,发现卵巢癌患者血清中KLK9水平显著升高,与肿瘤进展相关,表明其作为新型生物标志物的潜力。
3. **文献名称**:*Structural insights into KLK9 through recombinant protein crystallization and molecular dynamics*
**作者**:Egelund R, Petersen HH
**摘要**:通过重组KLK9蛋白的结晶和结构解析,揭示了其底物结合口袋的关键氨基酸残基,并模拟了其与抑制剂的相互作用,为靶向药物设计提供结构基础。
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**注**:以上内容基于KLK家族蛋白的常见研究方向模拟,实际文献需通过PubMed或Google Scholar等平台检索确认。
Kallikrein-related peptidase 9 (KLK9) is a member of the human kallikrein serine protease family, which comprises 15 secreted enzymes (KLK1-KLK15) encoded by a gene cluster on chromosome 19q13.4. KLK9 is expressed in various tissues, including the skin, brain, and reproductive organs, and is implicated in physiological processes such as tissue remodeling, hormone regulation, and inflammation. Structurally, KLK9 shares conserved catalytic triad residues (His, Asp, Ser) with other kallikreins and is synthesized as an inactive zymogen (pro-KLK9) that requires proteolytic cleavage for activation. Its enzymatic activity targets extracellular matrix proteins, growth factors, and other proteases, suggesting roles in cellular signaling and homeostasis.
Recombinant KLK9 protein is produced using expression systems like mammalian cells or bacteria, enabling controlled study of its biochemical properties and interactions. Researchers employ it to investigate KLK9's substrate specificity, regulatory mechanisms, and involvement in diseases. For instance, aberrant KLK9 expression has been linked to cancers (e.g., ovarian, breast) and neurodegenerative disorders, potentially serving as a diagnostic or prognostic biomarker. Recombinant KLK9 also aids in developing inhibitors or therapeutic antibodies, given its dysregulation in pathologies.
Despite progress, KLK9's precise physiological functions and regulatory pathways remain incompletely understood. Challenges include elucidating tissue-specific roles, cross-talk with other kallikreins, and context-dependent effects in disease. Recombinant protein tools continue to be vital for dissecting KLK9's contributions to cellular processes and its potential as a therapeutic target.
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