| 纯度 | >85% SDS-PAGE |
| 种属 | Human |
| 靶点 | BLVRB |
| Uniprot No | P30043 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-206aa |
| 氨基酸序列 | AVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY PSHQYQ |
| 预测分子量 | 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BLVRB重组蛋白的3篇代表性文献示例(注：内容为虚构，仅供格式参考)：
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1. **标题**: *"Efficient Expression and Purification of Recombinant Human BLVRB in Escherichia coli"*
**作者**: Zhang Y, et al.
**摘要**: 研究报道了利用大肠杆菌表达系统高效生产重组人BLVRB蛋白的方法，通过亲和层析纯化获得高活性蛋白，并验证其催化胆绿素还原为胆红素的功能。
2. **标题**: *"Structural Insights into Biliverdin Reductase B: Crystallographic Analysis of Recombinant BLVRB"*
**作者**: Lee S, et al.
**摘要**: 通过X射线晶体学解析了重组BLVRB蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，为设计靶向抑制剂提供了结构基础。
3. **标题**: *"Recombinant BLVRB Attenuates Oxidative Stress in Macrophages via Heme Metabolism Regulation"*
**作者**: Patel R, et al.
**摘要**: 利用重组BLVRB蛋白处理巨噬细胞，发现其通过调节血红素代谢通路减少活性氧(ROS)积累，提示其在炎症性疾病中的潜在治疗价值。
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**注**：如需真实文献，建议通过PubMed或Google Scholar检索关键词“BLVRB recombinant protein”获取最新研究。
**Background of BLVRB Recombinant Protein**
BLVRB (biliverdin reductase B) is a cytosolic enzyme integral to heme metabolism, primarily catalyzing the reduction of biliverdin IXβ to bilirubin IXβ using NADPH as a cofactor. This reaction is critical in the cellular antioxidant defense system, as bilirubin acts as a potent scavenger of reactive oxygen species (ROS). Beyond its role in heme degradation, BLVRB has been implicated in diverse cellular processes, including inflammation regulation, redox signaling, and mitochondrial function.
Structurally, BLVRB belongs to the flavin reductase family, characterized by a conserved Rossmann fold for NADPH binding. Its expression is ubiquitous but notably enriched in tissues with high metabolic activity, such as the liver and spleen. Recent studies have linked BLVRB dysregulation to pathological conditions, including neurodegenerative diseases, cancer, and metabolic disorders, highlighting its potential as a therapeutic target.
Recombinant BLVRB protein is engineered using heterologous expression systems (e.g., *E. coli*, mammalian cells) to ensure high purity and activity for research and clinical applications. Its production enables detailed biochemical studies, inhibitor screening, and exploration of its non-canonical roles, such as interactions with cellular kinases or transcriptional regulators. Additionally, recombinant BLVRB serves as a tool for developing diagnostic assays or therapies targeting oxidative stress-related diseases.
Overall, BLVRB recombinant protein bridges fundamental research and translational medicine, offering insights into cellular redox homeostasis and avenues for novel therapeutic strategies.
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