| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRXL2A |
| Uniprot No | Q9BRX8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-229aa |
| 氨基酸序列 | MSFLQDPSFFTMGMWSIGAGALGAAALALLLANTDVFLSKPQKAALEYLEDIDLKTLEKEPRTFKAKELWEKNGAVIMAVRRPGCFLCREEAADLSSLKSMLDQLGVPLYAVVKEHIRTEVKDFQPYFKGEIFLDEKKKFYGPQRRKMMFMGFIRLGVWYNFFRAWNGGFSGNLEGEGFILGGVFVVGSGKQGILLEHREKEFGDKVNLLSVLEAAKMIKPQTLASEKK |
| 预测分子量 | 33.2 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PRXL2A重组蛋白的参考文献示例(注：文献为模拟生成，实际引用需核实)：
1. **"Recombinant PRXL2A Protein Attenuates Oxidative Stress in Cardiomyocytes via Thioredoxin System Activation"**
*作者：Kim J, Park S, et al.*
摘要：本研究在大肠杆菌中成功表达并纯化重组人PRXL2A蛋白，证明其通过激活硫氧还蛋白系统降低心肌细胞氧化损伤，为心血管疾病治疗提供潜在靶点。
2. **"Structural Characterization of PRXL2A Reveals Unique Disulfide Reductase Activity"**
*作者：Chen X, Wang Q, et al.*
摘要：通过杆状病毒系统表达PRXL2A重组蛋白，利用X射线晶体学解析其三维结构，发现其新型二硫键还原酶活性，拓展了对过氧化物酶家族功能多样性的认知。
3. **"High-Yield Production of PRXL2A in Pichia pastoris and Its Neuroprotective Effects"**
*作者：Gomez-Ruiz B, et al.*
摘要：优化毕赤酵母表达系统实现PRXL2A高效分泌表达，动物实验显示重组蛋白能穿透血脑屏障，显著改善帕金森病模型小鼠的神经退行性病变。
(提示：实际文献建议通过PubMed/Google Scholar以关键词"PRXL2A recombinant"或结合其别名"PRDX2-like protein"检索，并关注其与氧化应激、癌症或神经疾病相关的研究。)
PRXL2A (Peroxiredoxin-like 2A), also known as PRDX2A, is a member of the peroxiredoxin family, a class of antioxidant enzymes critical for regulating cellular redox homeostasis. These proteins are primarily involved in scavenging reactive oxygen species (ROS), protecting cells from oxidative damage, and modulating redox-sensitive signaling pathways. PRXL2A shares structural homology with typical peroxiredoxins, featuring a conserved catalytic cysteine residue, but exhibits unique functional characteristics due to sequence variations in its active site. Unlike other peroxiredoxins, PRXL2A lacks peroxidase activity but retains the ability to interact with redox-regulated proteins, suggesting a regulatory role in oxidative stress responses.
Recombinant PRXL2A protein is engineered through heterologous expression systems, such as *E. coli* or mammalian cells, to produce purified, biologically active forms for research and therapeutic applications. Its production typically involves cloning the PRXL2A gene into expression vectors, followed by affinity chromatography (e.g., His-tag purification) and validation via SDS-PAGE or Western blot. Recombinant PRXL2A is widely used to study its non-catalytic functions, including interactions with apoptosis-related proteins (e.g., ASK1), modulation of the Nrf2-Keap1 antioxidant pathway, and involvement in mitochondrial integrity. Emerging studies highlight its potential role in neurodegenerative diseases, cancer, and metabolic disorders, where oxidative stress is a key contributor. For instance, PRXL2A overexpression has been linked to chemoresistance in certain cancers, while its downregulation correlates with neuronal damage in Alzheimer’s models. Despite lacking enzymatic activity, its regulatory mechanisms in redox signaling and protein-protein interactions make it a promising target for drug development. Current research focuses on elucidating its structural dynamics, post-translational modifications, and tissue-specific functions to harness its therapeutic potential in oxidative stress-related pathologies.
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