| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KLK8 |
| Uniprot No | O60259 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-260aa |
| 氨基酸序列 | QEDKVLGGHECQPHSQPWQAALFQGQQLLCGGVLVGGNWVLTAAHCKKPK YTVRLGDHSLQNKDGPEQEIPVVQSIPHPCYNSSDVEDHNHDLMLLQLRD QASLGSKVKPISLADHCTQPGQKCTVSGWGTVTSPRENFPDTLNCAEVKI FPQKKCEDAYPGQITDVMVCAGSSKGADTCQGDSGGPLVCDGALQGITSW GSDPCGRSDKPGVYTNICRYLDWIKKIIGSKG |
| 预测分子量 | 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3篇与KLK8重组蛋白相关的参考文献示例(注：内容基于领域内常见研究方向模拟，具体文献需通过数据库核实)：
1. **文献名称**：*Expression and purification of recombinant human kallikrein 8 in Escherichia coli for functional analysis*
**作者**：Yamasaki, K., et al.
**摘要**：该研究报道了利用大肠杆菌表达系统高效表达重组KLK8蛋白的优化方法，通过His标签纯化获得高活性蛋白，并验证了其对特定底物的蛋白酶活性。
2. **文献名称**：*KLK8-mediated proteolysis in synaptic plasticity and Alzheimer's disease pathology*
**作者**：Shimizu, T., et al.
**摘要**：文章探讨了重组KLK8蛋白在神经元中的功能，发现其通过切割神经细胞黏附分子参与突触可塑性调节，并与阿尔茨海默病中淀粉样蛋白代谢异常相关。
3. **文献名称**：*Structural characterization of recombinant KLK8 and its inhibition by synthetic peptides*
**作者**：Bayes-Genis, A., et al.
**摘要**：研究通过X射线晶体学解析了重组KLK8的三维结构，并筛选出特异性抑制其酶活性的合成多肽，为开发靶向KLK8的疾病治疗策略提供依据。
如需精准文献，建议通过PubMed或Web of Science检索关键词“recombinant KLK8”或“kallikrein 8 expression”。
Kallikrein-related peptidase 8 (KLK8), also known as neuropsin, is a serine protease encoded by the KLK8 gene in humans. It belongs to the kallikrein (KLK) family, which comprises 15 secreted serine proteases involved in diverse physiological processes, including tissue remodeling, inflammation, and neuronal signaling. KLK8 is primarily expressed in the brain, skin, and reproductive tissues. In the central nervous system, it plays a role in synaptic plasticity, learning, and memory by modulating extracellular matrix components and neuronal signaling pathways. Dysregulation of KLK8 has been implicated in neurological disorders such as Alzheimer’s disease and epilepsy, as well as in cancer progression, particularly in glioblastoma and metastatic cancers.
Recombinant KLK8 protein is engineered in vitro using expression systems like bacteria (E. coli), yeast, or mammalian cells to produce functional, purified enzymes for research and therapeutic applications. Its structure includes a catalytic triad (His, Asp, Ser) characteristic of serine proteases and a conserved N-terminal propeptide that is cleaved for activation. Recombinant KLK8 retains enzymatic activity, enabling studies on substrate specificity, inhibitor screening, and pathway analysis.
Research applications include investigating KLK8's role in neurodegenerative diseases, tumor microenvironment modulation, and epidermal barrier function. It also serves as a tool for developing diagnostic biomarkers or targeted therapies. Challenges in production involve maintaining proper post-translational modifications (e.g., glycosylation) critical for function, often addressed using mammalian expression systems. Overall, recombinant KLK8 provides a versatile platform for exploring its biological significance and translational potential.
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