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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MIA |
| Uniprot No | Q16674 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-131aa |
| 氨基酸序列 | GPMPKLADRK LCADQECSHP ISMAVALQDY MAPDCRFLTI HRGQVVYVFS KLKGRGRLFW GGSVQGDYYG DLAARLGYFP SSIVREDQTL KPGKVDVKTD KWDFYCQ |
| 预测分子量 | 12.1 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MIA(黑色素瘤抑制性活性蛋白)重组蛋白研究的参考文献示例(注：文献信息为示例，具体文献需通过学术数据库查询)：
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1. **标题**：*Structural and functional analysis of recombinant human MIA protein*
**作者**：Bosserhoff AK, et al.
**摘要**：通过X射线晶体学解析了重组MIA蛋白的三维结构，揭示了其与细胞外基质相互作用的SH3结构域特征，并验证了其在黑色素瘤细胞侵袭抑制中的功能。
2. **标题**：*MIA interacts with integrins to inhibit cell migration and metastasis*
**作者**：Stoll SW, et al.
**摘要**：研究重组MIA蛋白通过结合整合素受体(如α4β1)调控MAPK信号通路，抑制肿瘤细胞迁移和体内转移的分子机制。
3. **标题**：*Recombinant MIA as a biomarker in malignant melanoma progression*
**作者**：Gress TM, et al.
**摘要**：利用重组MIA蛋白开发ELISA检测方法，证实其在黑色素瘤患者血清中的表达水平与肿瘤分期及预后显著相关。
4. **标题**：*Expression and purification of bioactive MIA in Escherichia coli*
**作者**：Blesch A, et al.
**摘要**：优化大肠杆菌表达系统生产高纯度重组MIA蛋白，并通过体外实验证明其抑制神经轴突生长的活性。
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建议通过PubMed、Web of Science等平台搜索关键词“MIA recombinant protein”或“Melanoma Inhibitory Activity”获取具体文献。
Melanoma Inhibitory Activity (MIA) protein, first identified in the 1990s, is a small, secreted protein predominantly produced by malignant melanoma cells. It plays a critical role in tumor progression, metastasis, and immune evasion. Structurally, MIA belongs to the SH3 domain-containing protein family and consists of 131 amino acids with a molecular weight of approximately 11 kDa. Its unique fold, stabilized by two disulfide bonds, enables interactions with extracellular matrix components, such as fibronectin and integrins, facilitating tumor cell adhesion, migration, and invasion. MIA’s overexpression correlates with advanced melanoma stages and poor prognosis, making it a potential diagnostic and therapeutic target.
The development of recombinant MIA technology has enabled detailed functional studies and therapeutic exploration. Recombinant MIA is typically produced using bacterial (e.g., *E. coli*) or eukaryotic expression systems, ensuring proper folding and post-translational modifications for biological activity. Researchers employ it to dissect signaling pathways involved in melanoma metastasis, particularly its inhibition of apoptosis and promotion of tumor cell survival. Additionally, recombinant MIA serves as an antigen for antibody development, aiding in diagnostic assays and targeted therapies. Recent studies also explore its role beyond melanoma, including cartilage development and neurodegenerative diseases, highlighting its diverse biological functions.
Despite progress, challenges remain in fully understanding MIA’s pleiotropic effects and optimizing therapeutic strategies. Current research focuses on blocking MIA-integrin interactions or silencing its expression to inhibit metastasis. Its dual role as both a tumor promoter and tissue homeostasis regulator complicates therapeutic targeting, necessitating further mechanistic insights. Overall, recombinant MIA remains a vital tool in oncology research, bridging molecular understanding to clinical applications.
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