| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAGE4 |
| Uniprot No | O60829 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-102 aa |
| 活性数据 | MSARVRSRSR GRGDGQEAPD VVAFVAPGES QQEEPPTDNQ DIEPGQEREG TPPIEERKVE GDCQEMDLEK TRSERGDGSD VKEKTPPNPK HAKTKEAGDG QP |
| 分子量 | 11.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人PAGE4蛋白的3篇参考文献示例（基于公开研究背景概括，实际文献需通过学术数据库查询）：
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1. **文献名称**：*PAGE4 as a Stress-responsive Cancer/Testis Antigen: Phase Separation and Interaction with JNK Signaling*
**作者**：M. Kato et al.
**摘要**：研究揭示了重组人PAGE4蛋白作为一种内在无序蛋白（IDP），在细胞应激条件下通过液-液相分离（LLPS）调控JNK信号通路，可能在前列腺癌进展中发挥动态调控作用。
2. **文献名称**：*Expression and Purification of Recombinant PAGE4: Implications for Biomarker Development in Prostate Cancer*
**作者**：J. Smith et al.
**摘要**：报道了利用大肠杆菌系统高效表达和纯化重组PAGE4蛋白的方法，并验证其作为前列腺癌潜在生物标志物的可能性，通过血清学检测显示其在患者样本中显著上调。
3. **文献名称**：*The Role of PAGE4 in Androgen Receptor Signaling and Cellular Apoptosis Resistance*
**作者**：L. Chen et al.
**摘要**：探讨了重组PAGE4蛋白通过增强雄激素受体（AR）转录活性促进前列腺癌细胞抗凋亡能力的机制，为靶向PAGE4-AR轴的治疗策略提供理论依据。
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**注意**：以上为基于PAGE4已知研究方向的概括性示例，实际文献需通过PubMed、Google Scholar等平台检索。建议用户使用关键词“recombinant human PAGE4”、“PAGE4 cancer”、“PAGE4 phase separation”等进一步查阅具体研究。
**Background of Recombinant Human PAGE4 Protein**
Prostate-Associated Gene 4 (PAGE4) is a member of the cancer/testis antigen (CTA) family, primarily expressed in normal human tissues such as the prostate and testis. Its expression is frequently upregulated in prostate cancer and other malignancies, making it a potential biomarker and therapeutic target. PAGE4 is an intrinsically disordered protein (IDP), characterized by high structural flexibility, which enables dynamic interactions with diverse molecular partners. This plasticity allows PAGE4 to regulate stress-response pathways, including modulation of the Hippo signaling cascade and AP-1 transcription factor activity, influencing cell proliferation, apoptosis, and cancer progression.
Recombinant human PAGE4 protein is typically produced using bacterial or mammalian expression systems, facilitating studies on its structure-function relationships. Its disordered nature complicates structural characterization, but biophysical techniques (e.g., NMR spectroscopy) have revealed phosphorylation-dependent conformational changes that alter its biological activity. For instance, phosphorylated PAGE4 binds c-Jun, enhancing AP-1-driven transcriptional activity linked to prostate oncogenesis.
Research on recombinant PAGE4 also explores its role in cellular stress adaptation, hormone signaling, and immune evasion. Its restricted expression in normal tissues but overexpression in tumors highlights potential for immunotherapy or targeted therapies. However, challenges remain in understanding its precise mechanistic roles and clinical translation. Current studies focus on delineating PAGE4 interactions in tumor microenvironments and validating its utility in diagnostic or therapeutic strategies against prostate cancer.
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