| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | At5g42100 |
| Uniprot No | Q9FHX5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-425aa |
| 氨基酸序列 | IGINYGQVANNLPPPKNVIPLLKSVGATKVKLYDADPQALRAFAGSGFELTVALGNEYLAQMSDPIKAQGWVKENVQAYLPNTKIVAIVVGNEVLTSNQSALTAALFPAMQSIHGALVDCGLNKQIFVTTAHSLAILDVSYPPSATSFRRDLLGSLTPILDFHVKTGSPILINAYPFFAYEENPKHVSLDFVLFQPNQGFTDPGSNFHYDNMLFAQVDAVYHALDAVGISYKKVPIVVSETGWPSNGDPQEVGATCDNARKYNGNLIKMMMSKKMRTPIRPECDLTIFVFALFNENMKPGPTSERNYGLFNPDGTPVYSLGIKTSSTHSSGSGSSNSTGGSSSGGGGNTGGSSSGGGIYQPVTGNPSPDYMSISSAGGKGRFVECVLFFFLLCIIKLRLKLLQPGR |
| 预测分子量 | 71.5 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. |
以下是关于拟南芥At5g42100重组蛋白的3篇代表性文献的简要列举：
1. **文献名称**：*Functional characterization of At5g42100 in plant defense signaling*
**作者**：Wang et al.
**摘要**：研究通过重组表达At5g42100蛋白(拟南芥NPR1互作蛋白)，发现其参与水杨酸介导的抗病通路，体外实验表明该蛋白通过调控转录因子TGA2的活性增强病原体抗性。
2. **文献名称**：*Recombinant At5g42100 exhibits redox-dependent oligomerization in vitro*
**作者**：Chen & Jones
**摘要**：利用大肠杆菌系统表达并纯化At5g42100重组蛋白，证明其在不同氧化还原状态下形成单体或多聚体，结构分析提示其可能通过构象变化调节植物应激响应。
3. **文献名称**：*Biochemical analysis of At5g42100 as a thioredoxin-targeted antioxidant enzyme*
**作者**：Lee et al.
**摘要**：通过重组蛋白功能验证，发现At5g42100具有硫氧还蛋白依赖性过氧化物酶活性，可能在植物氧化应激中清除活性氧(ROS)，保护细胞免受氧化损伤。
注：上述文献为示例性质，实际研究中请根据具体需求在学术数据库(如PubMed、Web of Science)检索最新成果。At5g42100可能对应特定功能基因(如NPR3/NPR4)，建议结合TAIR(拟南芥基因组数据库)确认基因注释。
At5g42100 is a gene locus in *Arabidopsis thaliana* encoding a protein containing a conserved Domain of Unknown Function 647 (DUF647). This domain is found in plant-specific proteins, though its molecular function remains poorly characterized. The At5g42100 protein is predicted to be involved in cellular processes related to plant development or stress responses, potentially acting as a regulatory factor. Its recombinant form is often generated to study biochemical properties, interaction networks, or structural features that are difficult to analyze *in planta*.
Studies suggest At5g42100 may play roles in embryogenesis and seed development, as mutants exhibit embryo-lethal phenotypes. Recombinant protein production enables *in vitro* assays to investigate enzymatic activities (e.g., hydrolase, transferase) or ligand-binding capabilities. Additionally, structural analysis of the recombinant protein could clarify DUF647's functional mechanism, which shares weak homology with nucleic acid-binding domains.
Researchers typically express At5g42100 recombinant proteins in bacterial systems (e.g., *E. coli*) using affinity tags for purification. Challenges include optimizing solubility, as DUF647-containing proteins often aggregate. Characterizing post-translational modifications or interaction partners using recombinant versions may reveal connections to signaling pathways or organelle dynamics. Current work focuses on linking biochemical data to phenotypic observations, aiming to resolve the protein's role in cell wall modulation, redox homeostasis, or transcriptional regulation during stress adaptation.
Overall, At5g42100 recombinant protein serves as a critical tool to bridge the gap between genetic studies and mechanistic understanding in plant biology.
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