纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | KLK13 |
Uniprot No | Q9UKR3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 17-262aa |
氨基酸序列 | GGVSQESSKVLNTNGTSGFLPGGYTCFPHSQPWQAALLVQGRLLCGGVLV HPKWVLTAAHCLKEGLKVYLGKHALGRVEAGEQVREVVHSIPHPEYRRSP THLNHDHDIMLLELQSPVQLTGYIQTLPLSHNNRLTPGTTCRVSGWGTTT SPQVNYPKTLQCANIQLRSDEECRQVYPGKITDNMLCAGTKEGGKDSCEG DSGGPLVCNRTLYGIVSWGDFPCGQPDRPGVYTRVSRYVLWIRETIVDHH HHHH |
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. |
以下是关于KLK13重组蛋白的模拟参考文献示例(基于研究领域常见方向构造,非真实文献):
1. **文献名称**:*Expression and Functional Characterization of Recombinant KLK13 in Ovarian Cancer Models*
**作者**:Smith A., et al.
**摘要**:研究通过哺乳动物细胞系统表达重组KLK13蛋白,分析其蛋白酶活性及在卵巢癌细胞侵袭中的作用,揭示KLK13通过激活蛋白酶激活受体(PAR)促进肿瘤转移。
2. **文献名称**:*Purification and Biochemical Analysis of Recombinant KLK13: Substrate Specificity and pH-Dependent Activity*
**作者**:Chen L., Wang Y.
**摘要**:利用大肠杆菌系统表达并纯化重组KLK13.通过质谱和荧光底物实验确定其底物偏好性,发现KLK13在酸性环境下对细胞外基质蛋白水解活性显著增强。
3. **文献名称**:*Role of Recombinant KLK13 in Skin Barrier Homeostasis: Implications for Psoriasis Therapy*
**作者**:Rodriguez M., et al.
**摘要**:构建重组KLK13蛋白并验证其在人表皮角质形成细胞中的功能,证明其通过调节丝聚蛋白降解影响皮肤屏障修复,为银屑病治疗提供潜在靶点。
4. **文献名称**:*Structural Insights into Recombinant KLK13 via X-ray Crystallography*
**作者**:Tanaka K., et al.
**摘要**:首次解析重组KLK13的三维晶体结构,揭示其活性位点特征及与抑制剂的相互作用,为设计选择性KLK13抑制剂奠定结构基础。
注:以上文献为模拟内容,实际研究中建议通过学术数据库(如PubMed、Web of Science)检索真实文献。
Kallikrein-related peptidase 13 (KLK13) is a member of the human tissue kallikrein family, a group of 15 serine proteases (KLK1-KLK15) encoded by genes clustered on chromosome 19q13.4. These enzymes play diverse roles in physiological processes such as skin desquamation, semen liquefaction, and neuronal plasticity, as well as pathological conditions including inflammation and cancer. KLK13 is expressed in various tissues, including the thyroid, salivary glands, and reproductive organs, and is regulated by steroid hormones and epigenetic mechanisms. It exhibits trypsin-like enzymatic activity, cleaving substrates like extracellular matrix proteins and growth factors, influencing cellular signaling and tissue remodeling.
Recombinant KLK13 protein is produced using heterologous expression systems (e.g., Escherichia coli, mammalian cells) to enable functional studies. Its production typically involves codon optimization, affinity tag fusion (e.g., His-tag), and purification via chromatography. Recombinant KLK13 serves as a critical tool for investigating its biochemical properties, substrate specificity, and interactions with inhibitors. In cancer research, KLK13 shows dual roles: it acts as a biomarker in hormone-dependent cancers (e.g., breast, ovarian) and exhibits context-dependent expression—upregulated in some malignancies (e.g., esophageal squamous cell carcinoma) and downregulated in others. This dichotomy suggests tissue-specific regulatory mechanisms and potential therapeutic applications, such as targeting KLK13-mediated pathways or developing diagnostic assays.
Studies using recombinant KLK13 have also explored its involvement in neurodegenerative diseases and inflammatory disorders, highlighting its broader pathophysiological relevance. The protein’s structure-function relationships, including its catalytic triad and calcium-binding sites, remain active research areas. Overall, recombinant KLK13 provides a standardized platform for elucidating its biological roles and translational potential.
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