| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | PROLM25 |
| Uniprot No | P17048 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-156aa |
| 氨基酸序列 | RFDPLSQSYRQYQLQSHLLLQQQVLSPCSEFVRQQYSIVATPFWQPATFQLINNQVMQQQCCQQLRLVAQQSHYQAISIVQAIVQQLQLQQFSGVYFDQTQAQAQTLLTFNLPSICGIYPNYYSAPRSIATVGGVWY |
| 预测分子量 | 21.9 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PROLM25重组蛋白的模拟参考文献示例(注：内容为假设性概括，非真实文献)：
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1. **文献名称**: *"Heterologous Expression and Purification of PROLM25 in E. coli"*
**作者**: Smith A, et al.
**摘要**: 本研究报道了PROLM25重组蛋白在大肠杆菌中的高效表达及纯化策略。通过密码子优化和诱导条件优化，成功获得可溶性蛋白，并利用镍柱亲和层析纯化，为后续功能研究提供基础。
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2. **文献名称**: *"Structural Characterization of PROLM25 Using Cryo-EM"*
**作者**: Zhang L, et al.
**摘要**: 通过冷冻电镜技术解析了PROLM25的三维结构，揭示了其独特的螺旋-折叠结构域，并发现其与配体结合的潜在位点，为靶向药物设计提供了结构依据。
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3. **文献名称**: *"PROLM25 in Cancer Progression: Role and Mechanisms"*
**作者**: Lee J, et al.
**摘要**: 探讨了PROLM25在肿瘤细胞迁移和侵袭中的功能，发现其通过调控Wnt/β-catenin信号通路促进转移，重组蛋白的体外实验验证了其对细胞黏附的抑制作用。
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4. **文献名称**: *"Functional Analysis of PROLM25 Mutants in Neurodegeneration"*
**作者**: Johnson R, et al.
**摘要**: 构建了PROLM25的致病突变体重组蛋白，发现特定突变导致其错误折叠并引发神经细胞凋亡，提示其在神经退行性疾病中的潜在病理机制。
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如需真实文献，建议在PubMed或Web of Science中检索关键词“PROLM25 recombinant protein”或联系相关领域数据库。
PROLM25 is a recombinant protein engineered for research and potential therapeutic applications, designed to address specific biological questions or therapeutic needs. Derived from a naturally occurring protein, it is typically produced using heterologous expression systems such as *E. coli*, yeast, or mammalian cell cultures to ensure high purity and scalability. The "LM25" designation may reference its molecular weight (~25 kDa) or a functional domain within its structure, though precise nomenclature details often depend on the developer's conventions. Recombinant production enables precise control over post-translational modifications, enhancing stability and activity for experimental consistency.
Functionally, PROLM25 is hypothesized to interact with cellular receptors or signaling pathways, potentially involved in immune modulation, cell adhesion, or metabolic regulation. Its design might incorporate fusion tags (e.g., His-tag, FLAG) for purification or tracking, and structural features like disulfide bonds or glycosylation sites to mimic native folding. Studies may focus on its role in disease models, such as cancer progression, inflammatory responses, or infectious diseases, leveraging its recombinant nature to explore mechanistic pathways or therapeutic targeting.
In biomedical research, PROLM25 serves as a tool for *in vitro* assays, protein-protein interaction studies, or antibody development. Therapeutically, it could be explored as a biologic drug, vaccine component, or diagnostic biomarker. Current literature on PROLM25 remains limited, suggesting it is either emerging in preclinical studies or tailored for niche applications. Further characterization of its structure-function relationships, pharmacokinetics, and *in vivo* efficacy would solidify its translational potential. Overall, PROLM25 exemplifies the integration of recombinant protein technology to bridge molecular biology and applied medical science.
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