| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | POTEJ |
| Uniprot No | P0CG39 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1038aa |
| 氨基酸序列 | MVAEVDSMPAASSVKKPFVLRSKMGKWCRHCFPCCRGSGKSNVGTSGDQDDSTMKTLRSKMGKWCCHCFPCCRGSGKSNVGAWGDYDDSAFVEPRYHVRREDLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQRKSRTPENQQFPDNESEEYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSENGQPEKRSQEPEINKDGDRELENFMAIEEMKKHGSTHVGFPENLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCEEQNTGILHDEILIHEEKQIEVVEKMNSELSLSCKKERDFLHENSMLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTMDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF |
| 预测分子量 | 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POTEJ重组蛋白的3篇参考文献示例(部分信息为模拟生成，实际文献需通过学术数据库查询)：
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1. **文献名称**: "POTEJ Recombinant Protein Expression and Its Role in Cancer Cell Proliferation"
**作者**: Smith A, et al.
**摘要**: 本研究成功在大肠杆菌系统中表达了重组POTEJ蛋白，并验证其在前列腺癌细胞中的促增殖作用。研究发现，POTEJ通过激活Wnt/β-catenin通路增强肿瘤细胞的迁移和侵袭能力。
2. **文献名称**: "Structural Characterization of POTEJ as a Potential Tumor-Associated Antigen"
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析了POTEJ重组蛋白的三维结构，揭示了其特有的抗原表位。实验表明，POTEJ在乳腺癌和卵巢癌组织中高表达，提示其可作为免疫治疗的潜在靶点。
3. **文献名称**: "POTEJ Recombinant Protein Induces Antitumor Immune Response in Mouse Models"
**作者**: Wang Y, et al.
**摘要**: 利用重组POTEJ蛋白进行小鼠肿瘤模型免疫实验，结果显示其能显著激活T细胞免疫应答并抑制肿瘤生长，为基于POTEJ的癌症疫苗开发提供了实验依据。
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**注意**：以上为模拟示例，实际文献需通过PubMed、Web of Science等平台检索关键词(如"POTEJ recombinant protein")。若文献较少，可扩展检索至POTE家族其他成员(如POTEH、POTEE等)的研究。
The POTEJ recombinant protein is derived from the POTE gene family, a group of primate-specific genes that emerged through genomic duplication and diversification. These genes encode paralogs expressed in various tissues, with notable upregulation in cancers such as breast, prostate, and ovarian tumors. The POTE family is characterized by multiple tandem ankyrin repeat domains and a C-terminal cysteine-rich region, which are implicated in protein-protein interactions and cellular signaling. POTEJ, a specific isoform, shares these structural features but exhibits unique expression patterns and functional nuances.
Recombinant POTEJ is typically produced using eukaryotic expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications and structural fidelity. Its development stems from interest in its dual role as a tumor-associated antigen and a potential immune modulator. Studies suggest POTEJ overexpression in certain cancers correlates with disease progression, while its immunogenic epitopes may activate T-cell responses, positioning it as a candidate for cancer immunotherapy targets.
Research on POTEJ recombinant protein focuses on elucidating its biological functions, including its interplay with apoptotic pathways, immune evasion mechanisms, and interactions with oncogenic proteins like BRCA1. Challenges persist in decoding its exact molecular mechanisms due to splice variants and tissue-specific modifications. Current applications span diagnostic biomarker exploration, anticancer vaccine development, and functional studies using purified protein in vitro. Further investigation is needed to harness its therapeutic potential while addressing its structural complexity and evolutionary divergence from murine models.
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