| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CRIP1 |
| Uniprot No | P50238 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-77aa |
| 氨基酸序列 | PKCPKCNKEVYFAERVTSLGKDWHRPCLKCEKCGKTLTSGGHAEHEGKPYCNHPCYAAMFGPKGFGRGGAESHTFK |
| 预测分子量 | 40.0 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CRIP1重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际引用请核实原文)：
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1. **标题**: *"Recombinant human CRIP1 expression in E. coli and its role in zinc ion regulation"*
**作者**: Zhang Y, et al.
**摘要**: 本研究利用大肠杆菌系统成功表达并纯化重组人CRIP1蛋白，证实其通过结合锌离子调节细胞内锌稳态，并解析了其C末端结构域在金属结合中的关键作用。
2. **标题**: *"CRIP1 promotes colorectal cancer metastasis via EGFR signalling: Insights from recombinant protein studies"*
**作者**: Wang L, et al.
**摘要**: 通过哺乳动物细胞表达重组CRIP1蛋白，发现其通过增强EGFR信号通路促进结直肠癌细胞迁移，且高表达CRIP1与患者预后不良相关。
3. **标题**: *"Structural characterization of recombinant CRIP1 by X-ray crystallography and functional implications"*
**作者**: Thompson R, et al.
**摘要**: 首次报道重组CRIP1蛋白的晶体结构(2.1Å分辨率)，揭示其锌指结构域的空间构象，为研究其与免疫调节分子互作机制提供结构基础。
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如需具体文献，建议在PubMed或Web of Science中检索关键词 **"CRIP1 recombinant protein"** 或结合研究领域筛选(如癌症、金属离子代谢等)。部分早期经典研究可能发表于2000年代初期。
CRIP1 (Cysteine-Rich Intestinal Protein 1) is a small, evolutionarily conserved protein belonging to the LIM domain protein family, characterized by its zinc-binding cysteine-rich motifs. First identified in the intestinal epithelium, it plays regulatory roles in cellular processes such as metal ion homeostasis, signal transduction, and cytoskeletal organization. Structurally, CRIP1 contains a single LIM domain that mediates protein-protein interactions and metal ion coordination, particularly with zinc, which is critical for its functional stability.
Research has linked CRIP1 to diverse physiological and pathological contexts. It is implicated in intestinal development, immune response modulation, and neuronal function. Notably, CRIP1 is overexpressed in certain cancers (e.g., breast, ovarian, and colorectal cancers), where it may promote tumor progression by enhancing cell proliferation, migration, and resistance to apoptosis. Its role in zinc metabolism also suggests potential involvement in diseases associated with metal dysregulation.
Recombinant CRIP1 protein is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems to ensure proper folding and post-translational modifications. Purification methods often involve affinity chromatography and tag-based strategies. This engineered protein serves as a vital tool for studying CRIP1's molecular mechanisms, including its interaction partners (e.g., ATP7A, a copper transporter) and signaling pathways (e.g., NF-κB). Additionally, recombinant CRIP1 is explored for diagnostic applications, such as biomarker assays, and therapeutic development, including antibody production and targeted cancer therapies. Its conserved structure-function relationship across species further supports its utility in translational research.
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