| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UROD |
| Uniprot No | P06132 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-367aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN |
| 预测分子量 | 43 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UROD重组蛋白的参考文献示例(仅供格式参考，具体文献需通过学术数据库查询)：
1. **标题**：*Expression and Purification of Recombinant Human Uroporphyrinogen Decarboxylase in E. coli*
**作者**：Smith A, et al.
**摘要**：研究通过大肠杆菌表达系统成功克隆并纯化人源UROD重组蛋白，验证其酶活性，为卟啉症相关研究提供工具。
2. **标题**：*Crystal Structure of UROD from Saccharomyces cerevisiae*
**作者**：Lee B, et al.
**摘要**：解析了酵母源UROD重组蛋白的晶体结构，阐明其催化尿卟啉原脱羧的分子机制，助力酶学改造。
3. **标题**：*Recombinant UROD Therapy in a Mouse Model of Porphyria*
**作者**：Garcia R, et al.
**摘要**：评估重组UROD蛋白在卟啉症模型小鼠中的治疗效果，证明其可降低卟啉积累，具有潜在临床应用价值。
4. **标题**：*Optimization of UROD Production in Pichia pastoris*
**作者**：Chen H, et al.
**摘要**：优化毕赤酵母表达系统以提高UROD重组蛋白产量，并验证其稳定性和生物活性。
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**提示**：建议通过PubMed、Web of Science等平台以“UROD recombinant protein”“UROD expression”等关键词检索最新文献。
**Background of UROD Recombinant Protein**
Uroporphyrinogen decarboxylase (UROD) is a critical enzyme in the heme biosynthesis pathway, catalyzing the decarboxylation of uroporphyrinogen III to coproporphyrinogen III. This step is essential for the production of heme, a vital component of hemoglobin and cytochromes. Genetic mutations or deficiencies in UROD activity are linked to hepatic porphyrias, particularly porphyria cutanea tarda (PCT), a disorder characterized by skin lesions, photosensitivity, and hepatic dysfunction. Understanding UROD’s structure-function relationship and its role in disease pathogenesis has driven the development of recombinant UROD protein for research and therapeutic applications.
Recombinant UROD is produced using heterologous expression systems, such as *E. coli*, yeast, or mammalian cells, enabling large-scale purification of the enzyme with high homogeneity. Its production allows for detailed biochemical studies, including enzyme kinetics, substrate specificity, and interactions with inhibitors or modulators. Additionally, recombinant UROD serves as a tool for investigating molecular mechanisms underlying PCT, such as enzyme inactivation due to oxidative stress or iron overload.
In therapeutics, recombinant UROD has been explored for enzyme replacement therapy (ERT) to address UROD deficiencies. Preclinical studies suggest its potential to reduce toxic porphyrin accumulation in liver cells, alleviating disease symptoms. However, challenges remain in optimizing delivery methods and ensuring long-term stability *in vivo*. Beyond clinical applications, recombinant UROD is utilized in diagnostic assays to detect UROD inhibitors or screen for therapeutic compounds.
Current research focuses on engineering UROD variants with enhanced catalytic efficiency or resistance to oxidative inactivation, leveraging structural insights from crystallography and computational modeling. The development of recombinant UROD continues to bridge gaps in understanding porphyria pathophysiology and advancing targeted treatments for these rare metabolic disorders.
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