| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRSS21 |
| Uniprot No | Q9Y6M0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-288aa |
| 氨基酸序列 | IVGGEDAELGRWPWQGSLRLWDSHVCGVSLLSHRWALTAAHCFETYSDLSDPSGWMVQFGQLTSMPSFWSLQAYYTRYFVSNIYLSPRYLGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEALPSPHTLQEVQVAIINNSMCNHLFLKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQKLMAQS |
| 预测分子量 | 31.8 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PRSS21重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *Expression and functional characterization of recombinant PRSS21 (Testisin) in mammalian cells*
**作者**: Zhang Y, et al.
**摘要**: 该研究通过哺乳动物表达系统成功重组表达了PRSS21蛋白，并验证其丝氨酸蛋白酶活性。实验表明，重组PRSS21在体外能切割特定底物(如细胞外基质蛋白)，提示其在精子成熟或肿瘤微环境中的潜在作用。
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2. **文献名称**: *PRSS21 promotes tumor metastasis through regulation of EMT markers in ovarian cancer*
**作者**: Chen L, et al.
**摘要**: 研究利用重组PRSS21蛋白处理卵巢癌细胞，发现其通过激活蛋白酶激活受体(PAR)信号通路，诱导上皮-间质转化(EMT)，增强癌细胞侵袭能力，为PRSS21作为癌症治疗靶点提供依据。
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3. **文献名称**: *Purification and structural analysis of PRSS21 recombinant protein from Escherichia coli*
**作者**: Wang H, et al.
**摘要**: 通过大肠杆菌原核表达系统表达并纯化PRSS21重组蛋白，结合质谱和圆二色谱分析其二级结构，证实其酶活性依赖于正确的折叠及关键催化三联体(His/Asp/Ser)的完整性。
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(注：以上文献为虚拟示例，实际研究中建议通过PubMed或Sci-Hub等平台检索具体论文。)
PRSS21 (Protease Serine 21), also known as testisin or transmembrane protease serine 8 (TMPRSS8), is a glycosylphosphatidylinositol (GPI)-anchored serine protease belonging to the trypsin-like protease family. It was first identified in the late 1990s due to its predominant expression in testicular germ cells and certain cancer cells. Structurally, PRSS21 contains a conserved catalytic triad (His, Asp, Ser) essential for enzymatic activity and a unique N-terminal prodomain that undergoes proteolytic cleavage for activation. Unlike most serine proteases, PRSS21 is membrane-bound via GPI linkage, positioning it to interact with extracellular substrates and modulate cell surface processes.
Biologically, PRSS21 plays roles in tissue remodeling, inflammation, and cell signaling. It has been implicated in regulating sperm maturation and fertility in males. However, its dysregulation is associated with pathological conditions, particularly cancer. Overexpression of PRSS21 is observed in ovarian, leukemia, and melanoma cells, where it promotes tumor progression by activating proteolytic cascades, degrading extracellular matrix components, and facilitating metastasis. Its restricted normal tissue expression and cancer-specific upregulation make it a potential therapeutic target.
Recombinant PRSS21 protein is produced using eukaryotic expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications. The purified protein retains enzymatic activity and is widely used in functional studies, inhibitor screening, and structural analysis. Researchers employ it to investigate PRSS21's role in cancer biology, develop targeted therapies like monoclonal antibodies or small-molecule inhibitors, and explore diagnostic applications. Recent studies also suggest its involvement in immune evasion mechanisms, broadening its relevance in immunotherapy research. Despite progress, challenges remain in understanding its precise physiological substrates and regulatory pathways.
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