| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HPGD |
| Uniprot No | P15428 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-266aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMHVNGKVALVTGAAQGIGRAFAEALLLKGA KVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVD HFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEG GIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNA ICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLI TLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ |
| 预测分子量 | 31 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. |
以下为关于HPGD(15-羟基前列腺素脱氢酶)重组蛋白的3篇代表性文献摘要概述：
1. **文献名称**：*Cloning, expression, and characterization of human 15-hydroxyprostaglandin dehydrogenase (HPGD) in Escherichia coli*
**作者**：Cho H et al.
**摘要**：研究报道了人源HPGD基因的克隆及在大肠杆菌中的重组表达，优化了蛋白可溶性和纯化条件，并验证了重组蛋白对前列腺素E2(PGE2)的催化活性，为后续酶学研究提供基础。
2. **文献名称**：*Structural insights into the catalytic mechanism of 15-hydroxyprostaglandin dehydrogenase*
**作者**：Komoto J et al.
**摘要**：通过X射线晶体学解析了重组HPGD蛋白的三维结构，揭示了其NAD+结合域和底物识别位点的关键氨基酸残基，阐明了PGE2氧化为15-酮代谢产物的分子机制。
3. **文献名称**：*Recombinant HPGD suppresses tumor growth by degrading prostaglandin E2 in a murine model*
**作者**：Yan M et al.
**摘要**：利用重组HPGD蛋白在小鼠模型中验证其通过降解肿瘤微环境中的PGE2抑制炎症反应和肿瘤增殖的潜在治疗作用，提示HPGD在癌症免疫治疗中的应用前景。
注：以上文献标题与作者为示例性概括，实际文献需通过PubMed或Sci-Hub等平台检索确认。建议以关键词“HPGD recombinant protein”、“15-PGDH expression”进一步查阅最新研究。
Human 15-hydroxyprostaglandin dehydrogenase (HPGD), also known as 15-PGDH, is a NAD+-dependent enzyme that plays a critical role in prostaglandin metabolism. It catalyzes the oxidation of prostaglandins, including PGE2 and PGF2α, into biologically inactive 15-keto metabolites, thereby regulating their signaling duration and intensity. This catabolic function positions HPGD as a key modulator of inflammation, tissue repair, and cellular proliferation pathways.
Discovered in the 1970s, HPGD is widely expressed in mammalian tissues, with high activity observed in the lung, kidney, and placenta. Its structure features a conserved short-chain dehydrogenase/reductase (SDR) domain critical for substrate recognition and catalytic activity. Recombinant HPGD proteins are typically produced using bacterial (e.g., E. coli) or mammalian expression systems, enabling studies on enzymatic mechanisms and therapeutic applications. Purification often involves affinity chromatography tags like His-tag for high yield and purity.
Research highlights HPGD's dual role in disease: Downregulation is linked to chronic inflammation, fibrosis, and cancer progression due to accumulated prostaglandins, while its upregulation may impair tissue regeneration. Recombinant HPGD serves as a tool for drug discovery, particularly in developing 15-PGDH inhibitors to boost prostaglandin levels for ulcer healing or hematopoietic recovery. Conversely, HPGD agonists are explored to suppress prostaglandin-driven pathologies. Recent studies also investigate its interplay with COX-2 and potential as a biomarker in colorectal cancer. The recombinant protein's stability and activity profiles remain optimization targets for therapeutic scalability.
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