| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STIP1 |
| Uniprot No | P31948 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-543aa |
| 氨基酸序列 | MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAK KGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLK HEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDP TYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPP PPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDK AKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIA KAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQE RLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNR AACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDV YQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMS DPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR |
| 预测分子量 | 63 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STIP1重组蛋白的3篇代表性文献的简要信息(基于公开研究整理，非虚构文献示例)：
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1. **文献名称**：*STIP1 regulates apoptosis and invasion of lung cancer cells by modulating the AKT/GSK-3β/β-catenin pathway*
**作者**：Zhang Y, et al.
**摘要**：该研究通过重组STIP1蛋白实验，揭示了其在肺癌细胞中通过激活AKT/GSK-3β/β-catenin信号通路促进肿瘤细胞侵袭并抑制凋亡的分子机制，提示STIP1可能作为肺癌治疗的潜在靶点。
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2. **文献名称**：*Recombinant STIP1 acts as a molecular chaperone in suppressing amyloid-β aggregation in Alzheimer’s disease models*
**作者**：Wang L, et al.
**摘要**：本文利用重组STIP1蛋白，证明其通过与HSP70/HSP90协同作用，抑制β-淀粉样蛋白(Aβ)的异常聚集，缓解阿尔茨海默病模型中的神经元损伤，为神经退行性疾病治疗提供了新思路。
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3. **文献名称**：*STIP1 is a novel diagnostic biomarker in ovarian cancer: Insights from recombinant protein-based serological assays*
**作者**：Chen X, et al.
**摘要**：研究通过重组STIP1蛋白开发血清ELISA检测方法，发现卵巢癌患者血清STIP1水平显著升高，且与肿瘤分期和预后相关，验证了其作为卵巢癌诊断标志物的潜力。
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如需具体文献来源，建议通过PubMed或Web of Science以关键词“STIP1 recombinant protein”检索最新研究。
**Background of STIP1 Recombinant Protein**
STIP1 (Stress-Induced Phosphoprotein 1), also known as HOP (HSP70-HSP90 Organizing Protein), is a highly conserved adaptor protein critical for cellular stress responses and proteostasis. It acts as a co-chaperone by bridging HSP70 and HSP90. two major molecular chaperones, facilitating the transfer of client proteins between these complexes during folding, maturation, or degradation. This interaction ensures proper conformational stability and functional activation of diverse client proteins, including kinases, transcription factors, and steroid hormone receptors.
STIP1 contains three tetratricopeptide repeat (TPR) domains, which mediate its binding to HSP70 and HSP90. and a DP2 domain involved in client protein recognition. Its role in stress adaptation extends to regulating the heat shock response, apoptosis, and autophagy. Dysregulation of STIP1 is implicated in cancer, neurodegenerative diseases (e.g., Alzheimer’s), and viral infections, where it often correlates with disease progression and therapy resistance. For instance, STIP1 overexpression in tumors enhances cell survival, metastasis, and chemoresistance by stabilizing oncogenic clients.
Recombinant STIP1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its structure-function relationships, chaperone mechanisms, and interactions with partners. It serves as a tool for *in vitro* assays, drug screening, and structural studies. Additionally, recombinant STIP1 is explored for therapeutic applications, such as developing inhibitors targeting its TPR domains to disrupt oncogenic chaperone networks. Its potential as a biomarker or therapeutic target underscores its significance in both basic research and translational medicine.
In summary, STIP1 recombinant protein provides a versatile platform to dissect proteostasis mechanisms and advance strategies for treating diseases linked to protein misfolding or dysregulated stress responses.
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