| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMPRSS4 |
| Uniprot No | Q9NRS4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 54-437aa |
| 氨基酸序列 | KVILDKYYFLCGQPLHFIPRKQLCDGELDCPLGEDEEHCVKSFPEGPAVAVRLSKDRSTLQVLDSATGNWFSACFDNFTEALAETACRQMGYSSKPTFRAVEIGPDQDLDVVEITENSQELRMRNSSGPCLSGSLVSLHCLACGKSLKTPRVVGVEEASVDSWPWQVSIQYDKQHVCGGSILDPHWVLTAAHCFRKHTDVFNWKVRAGSDKLGSFPSLAVAKIIIIEFNPMYPKDNDIALMKLQFPLTFSGTVRPICLPFFDEELTPATPLWIIGWGFTKQNGGKMSDILLQASVQVIDSTRCNADDAYQGEVTEKMMCAGIPEGGVDTCQGDSGGPLMYQSDQWHVVGIVSWGYGCGGPSTPGVYTKVSAYLNWIYNVWKAEL |
| 预测分子量 | 49.8 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3篇关于TMPRSS4重组蛋白的参考文献摘要概括(基于近年研究主题)：
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1. **文献名称**: *TMPRSS4 promotes cancer cell proliferation and inhibits apoptosis via activation of the PI3K-AKT pathway in lung adenocarcinoma*
**作者**: Kim S, et al.
**摘要**: 该研究通过构建重组TMPRSS4蛋白，验证其在肺癌细胞中的促增殖和抗凋亡功能，证实其通过激活PI3K-AKT信号通路调控肿瘤进展，为靶向治疗提供依据。
2. **文献名称**: *TMPRSS4 is a cellular protease essential for influenza virus activation and pathogenesis*
**作者**: Lucas JM, et al.
**摘要**: 研究利用重组TMPRSS4蛋白及基因敲除模型，证明其在流感病毒包膜蛋白切割中的关键作用，揭示其通过促进病毒活化增强感染能力，提示其作为抗病毒靶点的潜力。
3. **文献名称**: *Structural characterization of TMPRSS4 and design of small-molecule inhibitors for pancreatic cancer therapy*
**作者**: Huang Y, et al.
**摘要**: 该研究通过重组表达并纯化TMPRSS4胞外域蛋白，解析其晶体结构，基于结构筛选出特异性小分子抑制剂，显著抑制胰腺癌细胞侵袭转移。
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**注**：以上文献为示例概括，实际文献需通过PubMed或Google Scholar检索确认。若需具体文献链接或全文，可提供更详细的研究方向或年份要求。
TMPRSS4 (Transmembrane Serine Protease 4) is a member of the type II transmembrane serine protease family, characterized by a conserved extracellular protease domain, a transmembrane region, and a short cytoplasmic tail. It is encoded by the *TMPRSS4* gene and is primarily expressed in epithelial tissues, where it plays roles in cellular adhesion, tissue remodeling, and proteolytic activation of substrates. Structurally, TMPRSS4 shares homology with other proteases like matriptase and hepsin, but it exhibits distinct substrate specificity and regulatory mechanisms.
Recombinant TMPRSS4 protein is engineered in vitro using expression systems (e.g., mammalian, insect, or bacterial cells) to produce the active protease domain or full-length protein for functional studies. This recombinant form allows researchers to investigate its enzymatic activity, substrate interactions, and role in physiological and pathological processes. Notably, TMPRSS4 has gained attention for its overexpression in cancers, including pancreatic, lung, and thyroid carcinomas, where it promotes tumor progression, metastasis, and resistance to therapy. Its proteolytic activity is linked to the activation of signaling pathways (e.g., PAR-2. integrins) and extracellular matrix degradation, facilitating cancer cell invasion.
Beyond oncology, TMPRSS4 is implicated in viral infections, such as influenza and SARS-CoV-2. by cleaving viral envelope proteins to enhance host cell entry. Recombinant TMPRSS4 serves as a tool to study these mechanisms and screen protease inhibitors. Challenges in its production include maintaining proper folding and post-translational modifications critical for activity. Current research focuses on developing TMPRSS4-targeted therapies, including monoclonal antibodies and small-molecule inhibitors, to disrupt its protumorigenic or proviral functions. Understanding its structure-function relationships through recombinant protein studies remains pivotal for advancing therapeutic strategies.
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