| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IMUP |
| Uniprot No | Q9GZP8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-85aa |
| 氨基酸序列 | MEFDLGAALEPTSQKPGVGAGHGGDPKLSPHKVQGRSEAGAGPGPKASNFRGLGKGRRLTAAPPSSKDTTALPTPAAAPAIRTRM |
| 预测分子量 | 35.5 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IMUP重组蛋白的模拟参考文献示例(非真实文献，供格式参考)：
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1. **标题**：*IMUP Recombinant Protein Enhances Anti-Tumor Immune Response in Breast Cancer Models*
**作者**：Zhang L, et al.
**摘要**：研究利用大肠杆菌表达系统成功获得高纯度IMUP重组蛋白，并验证其在乳腺癌小鼠模型中通过激活巨噬细胞和T细胞抑制肿瘤生长的免疫调节作用。
2. **标题**：*Expression and Purification of IMUP in CHO Cells: Implications for Therapeutic Development*
**作者**：Kim S, Patel R.
**摘要**：通过CHO细胞系统高效表达IMUP重组蛋白，优化纯化工艺，证明其稳定性及在体外抑制肺癌细胞迁移的潜在治疗价值。
3. **标题**：*Structural and Functional Characterization of IMUP Recombinant Protein in Inflammatory Signaling*
**作者**：Garcia M, et al.
**摘要**：利用X射线晶体学解析IMUP蛋白结构，揭示其通过结合TLR4受体抑制NF-κB通路，为炎症性疾病治疗提供新靶点。
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注：以上文献为示例，实际研究中请根据具体主题检索真实数据库(如PubMed、Web of Science)。
IMUP (Immunoglobulin-Mu-binding Protein), also known as PIP (Prolactin-Inducible Protein), is a small secretory protein encoded by the *SCGB2A2* gene. Initially identified in 1993 as a prolactin-responsive protein in breast cancer cells, IMUP has gained attention for its dual roles in physiological processes and disease progression. Structurally, it contains a conserved C-terminal domain similar to immunoglobulin-binding regions, enabling interactions with immune components like IgM and certain bacterial proteins.
In normal physiology, IMUP is expressed in exocrine tissues including salivary, lacrimal, and mammary glands, where it participates in mucosal immunity and epithelial differentiation. However, its overexpression has been documented in various cancers, particularly hormone-responsive malignancies like breast and prostate cancer. This cancer-associated upregulation correlates with tumor proliferation, angiogenesis, and metastasis through mechanisms involving matrix metalloproteinase activation and immune modulation.
The recombinant IMUP protein is typically produced using bacterial (E. coli) or mammalian expression systems, with molecular weights ranging from 14-17 kDa depending on glycosylation. Purification often involves affinity chromatography tags and refolding processes to maintain functional conformation. Current research focuses on its potential as a diagnostic biomarker and therapeutic target, particularly in cancer immunotherapy. Studies explore its role in tumor immune evasion through IgM binding and T-cell suppression, while other investigations examine its antimicrobial properties in mucosal surfaces. The protein's functional duality—acting as both an immune modulator and tumor promoter—makes it a compelling subject for translational research, though its precise molecular mechanisms remain partially characterized. Recent advances in structural biology and CRISPR-based functional studies are expected to clarify its pathophysiological roles and therapeutic applicability.
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