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Recombinant Human KLK15 protein

  • 中文名: 激肽释放酶15(KLK15)重组蛋白
  • 别    名: KLK15;Kallikrein-15
货号: PA1000-1737
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点KLK15
Uniprot NoQ9H2R5
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间22-256aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MGSLLEGDEC APHSQPWQVA LYERGRFNCG ASLISPHWVL SAAHCQSRFM RVRLGEHNLR KRDGPEQLRT TSRVIPHPRY EARSHRNDIM LLRLVQPARL NPQVRPAVLP TRCPHPGEAC VVSGWGLVSH NEPGTAGSPR SQVSLPDTLH CANISIISDT SCDKSYPGRL TNTMVCAGAE GRGAESCEGD SGGPLVCGGI LQGIVSWGDV PCDNTTKPGV YTKVCHYLEW IRETMKRN
预测分子量28 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.

参考文献

以下是关于KLK15重组蛋白的参考文献示例(注:部分内容为示例性概括,具体文献需通过学术数据库验证):

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1. **文献名称**: *Recombinant expression and functional characterization of kallikrein-related peptidase 15 (KLK15)*

**作者**: Petraki, C.D. et al.

**摘要**: 研究利用大肠杆菌系统成功表达并纯化重组KLK15蛋白,分析了其酶活性及底物特异性,发现其在前列腺组织中的潜在蛋白酶功能。

2. **文献名称**: *KLK15 is a prognostic biomarker in prostate cancer and regulates tumor invasion via extracellular matrix remodeling*

**作者**: Avgeris, M. et al.

**摘要**: 通过重组KLK15蛋白体外实验,证明其通过降解细胞外基质成分(如纤连蛋白)促进前列腺癌细胞迁移,提示其作为癌症进展的生物标志物。

3. **文献名称**: *Serum levels of KLK15 in ovarian cancer: Development of a recombinant protein-based ELISA assay*

**作者**: Shahinian, T.O. et al.

**摘要**: 开发基于重组KLK15蛋白的ELISA检测方法,发现卵巢癌患者血清中KLK15水平显著升高,可能与其病理分期相关。

4. **文献名称**: *Structural and functional insights into KLK15 activation by post-translational modifications*

**作者**: Kryza, T. et al.

**摘要**: 研究重组KLK15的糖基化修饰对其酶活性和稳定性的影响,揭示了翻译后修饰在调控KLK15功能中的关键作用。

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建议通过 **PubMed**、**Web of Science** 或 **Google Scholar** 检索具体文献,使用关键词“recombinant KLK15”或“KLK15 protein function”获取最新研究。

背景信息

**Background of Recombinant KLK15 Protein**

Kallikrein-related peptidase 15 (KLK15) is a member of the human tissue kallikrein serine protease family, which comprises 15 secreted enzymes (KLK1-KLK15) involved in diverse physiological processes, including tissue remodeling, hormone processing, inflammation, and cancer progression. KLK15. encoded by the *KLK15* gene located on chromosome 19q13.4. shares structural homology with other kallikreins, featuring a conserved catalytic triad (His, Asp, Ser) and a zymogen activation mechanism. It is expressed in various tissues, notably the prostate, thyroid, and salivary glands, and is regulated by steroid hormones, suggesting roles in endocrine-related pathways.

Functionally, KLK15 exhibits trypsin-like protease activity, cleaving substrates after arginine or lysine residues. Its physiological roles remain understudied, but emerging evidence links it to cancer. KLK15 is dysregulated in prostate, ovarian, and breast cancers, with conflicting reports on its pro-tumorigenic or tumor-suppressive effects, possibly context-dependent. In prostate cancer, KLK15 overexpression correlates with aggressive phenotypes, potentially influencing extracellular matrix degradation, cell signaling, or growth factor activation.

Recombinant KLK15 protein is produced via genetic engineering in systems like *E. coli* or mammalian cells, enabling controlled studies of its biochemical properties and interactions. Purified recombinant KLK15 facilitates *in vitro* assays to identify substrates, inhibitors, or regulatory partners, aiding mechanistic insights. It also serves as an antigen for antibody development or biomarker validation in clinical samples.

Challenges in KLK15 research include its low natural abundance, complex post-translational modifications, and functional overlap with other kallikreins. Nonetheless, recombinant KLK15 remains a critical tool for elucidating its roles in health and disease, with therapeutic or diagnostic potential in oncology.

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