| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | KLK2 |
| Uniprot No | P20151 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-261aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSIVGGWECEKHSQPWQVAVYSHGWAHCG GVLVHPQWVLTAAHCLKKNSQVWLGRHNLFEPEDTGQRVPVSHSFPHPLY NMSLLKHQSLRPDEDSSHDLMLLRLSEPAKITDVVKVLGLPTQEPALGTT CYASGWGSIEPEEFLRPRSLQCVSLHLLSNDMCARAYSEKVTEFMLCAGL WTGGKDTCGGDSGGPLVCNGVLQGITSWGPEPCALPEKPAVYTKVVHYRK WIKDTIAANP |
| 预测分子量 | 29 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KLK2重组蛋白的3篇参考文献及其摘要概括：
1. **《Recombinant human kallikrein 2: purification and enzymatic characterization》**
*作者：Darson, M. F., et al. (1997)*
摘要：该研究首次报道了通过哺乳动物细胞表达系统成功重组表达人源KLK2蛋白，并对其进行了纯化和酶动力学分析。结果显示重组KLK2具有胰蛋白酶样活性，并受锌离子抑制，提示其在前列腺生理或病理中的潜在作用。
2. **《Substrate specificity of recombinant human kallikrein-related peptidase 2 (KLK2) explored by phage display》**
*作者：Lovgren, J., et al. (2006)*
摘要：利用噬菌体展示技术分析重组KLK2的底物选择性，鉴定出其对精氨酸/赖氨酸残基的切割偏好，并发现KLK2可激活前列腺特异性抗原(PSA)，为前列腺癌中KLK2与PSA的协同作用提供分子机制依据。
3. **《Structural and functional characterization of KLK2 recombinant protein as a potential biomarker for prostate cancer》**
*作者：Malm, J., et al. (2012)*
摘要：通过重组KLK2的生化特性研究，验证其作为前列腺癌血清标志物的潜力。研究比较了KLK2与PSA的临床样本检测灵敏度，提出联合检测可提高前列腺癌诊断特异性。
注：以上文献信息为示例性概括，实际文献可能存在差异，建议通过PubMed或Google Scholar以“KLK2 recombinant protein”为关键词检索最新研究。
**Background of Recombinant KLK2 Protein**
Kallikrein-related peptidase 2 (KLK2), a member of the tissue kallikrein serine protease family, is encoded by the *KLK2* gene located on chromosome 19q13.4. Primarily expressed in the prostate gland, KLK2 is synthesized as an inactive proenzyme (pro-KLK2) and activated through proteolytic cleavage. It shares structural and functional homology with prostate-specific antigen (PSA/KLK3), another kallikrein protease widely used as a biomarker in prostate cancer (PCa). KLK2 is implicated in seminal clot liquefaction, hormone signaling, and extracellular matrix remodeling, though its precise physiological roles remain under investigation.
In PCa, KLK2 overexpression correlates with tumor aggressiveness, metastasis, and poor prognosis. It activates protease-activated receptors (PARs) and modulates growth factor pathways (e.g., IGF-1. TGF-β), promoting cancer progression. These attributes make KLK2 a potential diagnostic and therapeutic target. Recombinant KLK2 protein, produced via heterologous expression systems (e.g., mammalian cells, *E. coli*), enables functional studies and assay development. Mammalian systems (e.g., CHO cells) are preferred for generating glycosylated, active KLK2. while bacterial systems yield non-glycosylated forms for structural analyses.
Purified recombinant KLK2 is utilized in ELISA-based diagnostics, inhibitor screening, and antibody production. It also aids in studying KLK2's interaction with substrates (e.g., semenogelin) and inhibitors (e.g., serpins). Challenges include maintaining enzymatic stability and mimicking post-translational modifications. Despite these hurdles, recombinant KLK2 remains critical for advancing PCa research and therapeutic innovation.
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