| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Tmprss15 |
| Uniprot No | P98073 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1019aa |
| 氨基酸序列 | MGSKRGISSRHHSLSSYEIMFAALFAILVVLCAGLIAVSCLTIKESQRGAALGQSHEARATFKITSGVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQWVSDENVKEELIQGLEANKSSQLVTFHIDLNSVDILDKLTTTSHLATPGNVSIECLPGSSPCTDALTCIKADLFCDGEVNCPDGSDEDNKMCATVCDGRFLLTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYTDILDIYEGVGSSKILRASIWETNPGTIRIFSNQVTATFLIESDESDYVGFNATYTAFNSSELNNYEKINCNFEDGFCFWVQDLNDDNEWERIQGSTFSPFTGPNFDHTFGNASGFYISTPTGPGGRQERVGLLSLPLDPTLEPACLSFWYHMYGENVHKLSINISNDQNMEKTVFQKEGNYGDNWNYGQVTLNETVKFKVAFNAFKNKILSDIALDDISLTYGICNGSLYPEPTLVPTPPPELPTDCGGPFELWEPNTTFSSTNFPNSYPNLAFCVWILNAQKGKNIQLHFQEFDLENINDVVEIRDGEEADSLLLAVYTGPGPVKDVFSTTNRMTVLLITNDVLARGGFKANFTTGYHLGIPEPCKADHFQCKNGECVPLVNLCDGHLHCEDGSDEADCVRFFNGTTNNNGLVRFRIQSIWHTACAENWTTQISNDVCQLLGLGSGNSSKPIFPTDGGPFVKLNTAPDGHLILTPSQQCLQDSLIRLQCNHKSCGKKLAAQDITPKIVGGSNAKEGAWPWVVGLYYGGRLLCGASLVSSDWLVSAAHCVYGRNLEPSKWTAILGLHMKSNLTSPQTVPRLIDEIVINPHYNRRRKDNDIAMMHLEFKVNYTDYIQPICLPEENQVFPPGRNCSIAGWGTVVYQGTTANILQEADVPLLSNERCQQQMPEYNITENMICAGYEEGGIDSCQGDSGGPLMCQENNRWFLAGVTSFGYKCALPNRPGVYARVSRFTEWIQSFLH |
| 预测分子量 | 112,9 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Tmprss15重组蛋白的3篇代表性文献信息(部分内容基于模拟数据，建议通过学术数据库验证)：
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1. **文献名称**: "Recombinant Expression and Functional Characterization of Human Tmprss15 in Intestinal Enzyme Activation"
**作者**: Smith A, et al.
**摘要**: 研究报道了利用HEK293细胞系统成功表达重组人Tmprss15蛋白，证实其作为肠肽酶原激活关键酶的功能，并分析其底物特异性及pH依赖性活性。
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2. **文献名称**: "Tmprss15 Knockout Mice Reveal Its Role in Pancreatic Protease Maturation"
**作者**: Tanaka K, et al.
**摘要**: 通过构建Tmprss15基因敲除小鼠模型，结合重组蛋白回补实验，阐明Tmprss15在胰腺外分泌功能中调控胰蛋白酶原激活的分子机制。
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3. **文献名称**: "Structural Insights into Tmprss15 via Cryo-EM: Implications for Substrate Binding"
**作者**: Chen L, et al.
**摘要**: 利用冷冻电镜解析重组Tmprss15蛋白的三维结构，揭示其底物结合域的关键氨基酸残基，为设计靶向抑制剂提供结构生物学基础。
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注：以上文献信息为示例性质，实际研究中建议通过PubMed、Google Scholar等平台以“Tmprss15 recombinant protein”或“TMPRSS15 expression”为关键词检索最新论文。
Tmprss15. also known as enteropeptidase or enterokinase, is a type II transmembrane serine protease primarily recognized for its critical role in intestinal digestion. It is synthesized as a zymogen and expressed predominantly in the duodenal mucosa, where it activates trypsinogen by cleaving its N-terminal propeptide, initiating the proteolytic cascade of pancreatic enzymes. Structurally, Tmprss15 consists of an N-terminal transmembrane domain, a stem region, and a C-terminal catalytic domain with a conserved serine protease triad (His, Asp, Ser). Its specificity for the cleavage motif (Asp-Asp-Asp-Asp-Lys) makes it indispensable in both physiological digestion and recombinant protein production.
Recombinant Tmprss15 is engineered to mimic the native enzyme's catalytic activity while optimizing solubility and stability for laboratory and therapeutic applications. Produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells), the recombinant form often excludes the transmembrane domain to generate a secreted, soluble protein. This modification facilitates its use in vitro for activating trypsinogen in diagnostic assays or processing fusion proteins in biopharmaceutical manufacturing. Additionally, recombinant Tmprss15 has therapeutic potential in treating enteropeptidase deficiency, a rare disorder impairing nutrient absorption.
Recent studies also explore its involvement in cellular signaling and disease pathways, including cancer metastasis and viral entry mechanisms (e.g., SARS-CoV-2), though these roles remain under investigation. The development of recombinant Tmprss15 continues to advance research in enzymology, drug development, and molecular biology, highlighting its versatility beyond traditional digestive functions.
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