| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRF |
| Uniprot No | P06850 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 43-196aa |
| 氨基酸序列 | LDFFQPPPQSEQPQQPQARPVLLRMGEEYFLRLGNLNKSPAAPLSPASSL LAGGSGSRPSPEQATANFFRVLLQQLLLPRRSLDSPAALAERGARNALGG HQEAPERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEI IGK |
| 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3篇与CRF(促肾上腺皮质激素释放因子)重组蛋白相关的文献示例及其摘要：
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1. **文献名称**: *Optimization of CRF Recombinant Protein Expression in E. coli for Neuroendocrine Studies*
**作者**: Zhang et al., 2020
**摘要**: 研究通过优化大肠杆菌表达系统，成功实现人源CRF重组蛋白的高效可溶性表达，并验证其生物活性可用于体外神经内分泌信号通路研究。
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2. **文献名称**: *Structural and Functional Analysis of CRF Receptor-Binding Domains Using Recombinant Protein Fragments*
**作者**: Thompson & Lee, 2018
**摘要**: 通过重组技术表达CRF蛋白的不同功能域片段，结合X射线晶体学揭示CRF与其受体相互作用的关键结构位点，为靶向药物设计提供依据。
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3. **文献名称**: *CRF Recombinant Protein Purification via Affinity Chromatography: A Comparative Study*
**作者**: Gupta et al., 2015
**摘要**: 对比多种亲和层析方法纯化CRF重组蛋白的效率，提出基于His标签和离子交换联用的策略，显著提高蛋白纯度和产量。
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4. **文献名称**: *CRF Overexpression in Transgenic Mice Alters Stress Response Pathways*
**作者**: Müller et al., 2010
**摘要**: 利用重组CRF蛋白建立的转基因小鼠模型，揭示了CRF过度表达与下丘脑-垂体-肾上腺轴(HPA轴)异常激活的关联，助力焦虑症机制研究。
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注：以上文献信息为示例，实际引用时需核对真实文献来源及细节。
**Background of CRF Recombinant Proteins**
Corticotropin-releasing factor (CRF), also known as corticotropin-releasing hormone (CRH), is a neuropeptide central to regulating the hypothalamic-pituitary-adrenal (HPA) axis, a critical system in stress response and homeostasis. Discovered in the 1980s, CRF acts as a primary mediator of endocrine, behavioral, and autonomic responses to stressors by stimulating adrenocorticotropic hormone (ACTH) release from the pituitary gland. Dysregulation of CRF signaling is implicated in various disorders, including anxiety, depression, and metabolic syndromes, making it a pivotal target for biomedical research.
Recombinant CRF proteins are engineered using genetic engineering techniques to produce purified, biologically active forms of the peptide. These proteins are synthesized in heterologous expression systems, such as *E. coli* or mammalian cell lines, by inserting the CRF gene into plasmid vectors for controlled expression. Recombinant technology enables scalable production with high consistency, overcoming limitations of natural extraction methods, which often yield low quantities and variable purity.
CRF recombinant proteins are widely utilized in both basic and applied research. They facilitate studies on CRF receptor interactions, downstream signaling pathways, and the molecular basis of stress-related pathologies. Additionally, they serve as tools for drug discovery, aiding in the development of CRF receptor antagonists as potential therapeutics for psychiatric and inflammatory disorders. Their application extends to diagnostic assays, where they act as standards or antigens to measure CRF levels in clinical samples.
The development of recombinant CRF variants, including species-specific or modified forms (e.g., tagged or fluorescently labeled proteins), has further expanded experimental flexibility. By providing precise control over protein structure and function, recombinant CRF proteins continue to drive advances in understanding stress biology and developing targeted therapies.
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