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| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRL8A4 |
| Uniprot No | P33580 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-239aa |
| 氨基酸序列 | IPACMVEEG DCWDPLQETF NSAIQRAETL CNLADQLYVE FYQNQFSSRQ FADLNSKLIK RDETVLKAGI YCHSTLAKPQ TRGGNFEIEE HLKMLINFVG SWISPLFHLV IELSAMEGVP ETILCKVKDL EENNRQLLDD LRWILTKVSP TAEIREEFPS WEHLSFLKSS NKNNKFLAMF NLSNCLDNDT KFTLHHLRIF KCLITGKDC |
| 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PRL8A4重组蛋白的模拟参考文献示例(注：PRL8A4可能为假设或特定研究中的命名，实际文献需通过数据库验证)：
1. **《重组PRL8A4蛋白的表达、纯化及其在肝癌细胞侵袭中的作用》**
- 作者：Zhang Y, et al.
- 摘要：本研究通过大肠杆菌系统成功表达并纯化重组PRL8A4蛋白，证实其在体外促进肝癌细胞迁移和侵袭，可能与调节MAPK信号通路相关。
2. **《PRL8A4重组蛋白的晶体结构及其磷酸酶活性分析》**
- 作者：Wang L, et al.
- 摘要：首次解析了PRL8A4重组蛋白的三维结构，揭示其活性位点特征，并通过酶活实验证明其对磷酸酪氨酸的特异性水解功能。
3. **《基于PRL8A4重组蛋白的肿瘤诊断抗体开发》**
- 作者：Chen X, et al.
- 摘要：利用重组PRL8A4蛋白制备单克隆抗体，验证其在结直肠癌患者血清中的高表达，提示其作为生物标志物的潜力。
4. **《PRL8A4重组蛋白在肿瘤免疫治疗中的靶向效应研究》**
- 作者：Kim S, et al.
- 摘要：构建PRL8A4重组蛋白-纳米颗粒复合物，通过体内实验证明其抑制肿瘤生长并增强T细胞抗肿瘤免疫应答。
**建议**：实际研究中请通过PubMed、Web of Science等平台，以“PRL8A4 recombinant protein”或相关关键词检索最新文献，并核对目标蛋白命名是否准确(如PRL-3/PTP4A3等类似家族蛋白的研究可能更常见)。
**Background of PRL8A4 Recombinant Protein**
PRL8A4 is a recombinant protein whose name likely derives from its association with the phosphatase of regenerating liver (PRL) family or a related classification system. While detailed public data on PRL8A4 remains limited, proteins in the PRL family are typically small, prenylated phosphatases implicated in cellular processes such as proliferation, migration, and metastasis. PRL members (e.g., PRL-1. PRL-2. PRL-3) are often overexpressed in cancers and linked to poor prognosis, making them potential therapeutic targets.
As a recombinant protein, PRL8A4 is likely produced through genetic engineering, expressed in host systems like *E. coli* or mammalian cells, and purified for research applications. Recombinant technology enables precise control over protein structure, ensuring consistency for functional studies. PRL8A4 may serve as a tool to investigate signaling pathways, protein-protein interactions, or enzymatic activity in vitro or in vivo.
If PRL8A4 shares functional parallels with other PRL phosphatases, it might regulate MAPK, PI3K/Akt, or other oncogenic pathways. Its recombinant form could be used to develop antibodies, screen inhibitors, or study mechanisms underlying diseases like cancer or metabolic disorders. However, specific roles of PRL8A4 require validation through peer-reviewed studies, as nomenclature variations and unpublished data may obscure its exact biological context.
In summary, PRL8A4 represents a engineered protein with potential relevance to cellular regulation and disease mechanisms, warranting further characterization to clarify its unique functions and applications in biomedical research.
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