| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PREB |
| Uniprot No | Q9HCU5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-388aa |
| 氨基酸序列 | MGRRRAPELYRAPFPLYALQVDPSTGLLIAAGGGGAAKTGIKNGVHFLQLELINGRLSASLLHSHDTETRATMNLALAGDILAAGQDAHCQLLRFQAHQQQGNKAEKAGSKEQGPRQRKGAAPAEKKCGAETQHEGLELRVENLQAVQTDFSSDPLQKVVCFNHDNTLLATGGTDGYVRVWKVPSLEKVLEFKAHEGEIEDLALGPDGKLVTVGRDLKASVWQKDQLVTQLHWQENGPTFSSTPYRYQACRFGQVPDQPAGLRLFTVQIPHKRLRQPPPCYLTAWDGSNFLPLRTKSCGHEVVSCLDVSESGTFLGLGTVTGSVAIYIAFSLQCLYYVREAHGIVVTDVAFLPEKGRGPELLGSHETALFSVAVDSRCQLHLLPSRRS |
| 预测分子量 | 49.8 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PREB重组蛋白的假设性参考文献示例(仅供参考，具体文献需核实)：
1. **《Cloning and Functional Analysis of Human PREB as a Transcriptional Regulator》**
- 作者：Shimizu, K. et al.
- 摘要：研究通过重组技术表达人源PREB蛋白，证实其特异性结合催乳素基因调控元件(PRER)，并激活下游基因转录，揭示其在激素调控中的作用。
2. **《Interaction of PREB with SEC31 in Vesicle Trafficking Pathways》**
- 作者：Tanaka, M. et al.
- 摘要：利用重组PREB蛋白进行互作实验，发现其与内质网-高尔基体转运蛋白SEC31结合，提示PREB可能参与分泌途径的调控。
3. **《Structural Characterization of Recombinant PREB by X-ray Crystallography》**
- 作者：Shibata, H. et al.
- 摘要：解析重组PREB蛋白的晶体结构，揭示其DNA结合域的关键氨基酸残基，为功能研究提供结构基础。
4. **《PREB Modulates Cellular Stress Response via ER Signaling》**
- 作者：Hirose, T. et al.
- 摘要：研究表明重组PREB蛋白在内质网应激条件下表达上调，并通过调控未折叠蛋白反应(UPR)相关基因影响细胞存活。
**注意**：以上为示例性内容，实际文献需通过学术数据库(如PubMed、Google Scholar)检索确认。
**Background of PREB Recombinant Protein**
The PREB (Prolactin Regulatory Element Binding) protein is a transcription factor initially identified for its role in regulating prolactin gene expression by binding to specific DNA sequences in the prolactin promoter. It belongs to the SEC14-like family of proteins, characterized by a conserved SEC14 domain, which often mediates lipid binding or sensing. PREB is involved in diverse cellular processes, including transcriptional regulation, metabolic signaling, and secretory pathway modulation.
Structurally, PREB contains functional domains that enable interactions with DNA, other proteins, and possibly lipids. Studies suggest its involvement in broader physiological contexts beyond prolactin regulation, such as adipocyte differentiation, glucose homeostasis, and neuronal function. Dysregulation of PREB has been linked to metabolic disorders, including obesity and insulin resistance, highlighting its potential as a therapeutic target.
Recombinant PREB protein is engineered using expression systems like *E. coli* or mammalian cells, followed by purification via affinity chromatography. This allows researchers to study its biochemical properties, molecular interactions, and structural features *in vitro*. Applications include elucidating PREB’s role in gene networks, screening for binding partners or inhibitors, and developing assays to probe its activity in disease models.
Recent research also explores PREB’s interplay with signaling pathways like cAMP and mTOR, emphasizing its integrative role in cellular responses to nutrient availability and hormonal cues. As a tool, recombinant PREB advances understanding of transcription mechanisms and metabolic regulation, offering insights for biomedical interventions in endocrine and metabolic diseases.
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