| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRSS27 |
| Uniprot No | Q9BQR3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-290aa |
| 氨基酸序列 | MVGGQDTQEGEWPWQVSIQRNGSHFCGGSLIAEQWVLTAAHCFRNTSETSLYQVLLGARQLVQPGPHAMYARVRQVESNPLYQGTASSADVALVELEAPVPFTNYILPVCLPDPSVIFETGMNCWVTGWGSPSEEDLLPEPRILQKLAVPIIDTPKCNLLYSKDTEFGYQPKTIKNDMLCAGFEEGKKDACKGDSGGPLVCLVGQSWLQAGVISWGEGCARQNRPGVYIRVTAHHNWIHRIIPKLQFQPARLGGQK |
| 预测分子量 | 35.1kDa |
| 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PRSS27重组蛋白的3篇参考文献及其简要摘要：
1. **文献名称**：*Recombinant PRSS27 Expression and Enzymatic Characterization in Tumor Microenvironments*
**作者**：Antalis TM, et al.
**摘要**：该研究成功表达并纯化了重组PRSS27蛋白，分析了其在肿瘤微环境中的丝氨酸蛋白酶活性，发现其通过降解细胞外基质成分促进肿瘤细胞侵袭。
2. **文献名称**：*Structural Insights into PRSS27 Protease Activation and Substrate Specificity*
**作者**：Chen L, Zhang Y
**摘要**：通过X射线晶体学解析了重组PRSS27的3D结构，揭示了其酶活性中心的构象变化及底物结合特性，为设计特异性抑制剂提供结构基础。
3. **文献名称**：*PRSS27 Knockout and Recombinant Rescue in Mouse Embryonic Development*
**作者**：Smith J, et al.
**摘要**：利用基因敲除小鼠模型，证明PRSS27缺失导致胚胎发育异常，而外源重组PRSS27蛋白可部分恢复胚胎组织分化和血管生成功能。
(注：上述文献为示例性概括，实际引用需根据具体研究补充真实文献信息。)
PRSS27. also known as epithin or matriptase-3. is a member of the type II transmembrane serine protease family. It is encoded by the PRSS27 gene in humans and plays roles in extracellular matrix remodeling, cellular signaling, and tissue homeostasis. Structurally, PRSS27 consists of a cytoplasmic domain, a transmembrane region, and an extracellular serine protease domain. Its enzymatic activity relies on a catalytic triad (His, Asp, Ser) common to serine proteases.
Functionally, PRSS27 is implicated in skin differentiation, inflammation, and cancer progression. Studies suggest it activates proteolytic cascades by cleaving substrates such as prostasin, influencing epidermal barrier formation. In pathological contexts, PRSS27 exhibits dual roles: it may promote tumor invasion by degrading extracellular matrix components or act as a tumor suppressor through regulatory cleavage of growth factors. Dysregulation of PRSS27 has been linked to inflammatory skin disorders (e.g., psoriasis) and malignancies (e.g., breast and colorectal cancers).
Recombinant PRSS27 protein is produced using expression systems (e.g., mammalian HEK293 or bacterial cells) to enable functional studies. The purified protein retains enzymatic activity and is used to investigate substrate specificity, inhibitor screening, and signaling pathways. Its applications extend to developing therapeutic antibodies or small-molecule inhibitors targeting PRSS27-associated diseases. Challenges in research include understanding tissue-specific regulation, interaction networks, and its paradoxical roles in cancer. Current efforts focus on elucidating PRSS27's physiological mechanisms and validating its potential as a diagnostic biomarker or therapeutic target.
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