| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLEKHB2 |
| Uniprot No | Q96CS7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MAFVKSGWLLRQSTILKRWKKNWFDLWSDGHLIYYDDQTRQNIEDKVHMPMDCINIRTGQECRDTQPPDGKSKDCMLQIVCRDGKTISLCAESTDDCLAWKFTLQDSRTNTAYVGSAVMTDETSVVSSPPPYTAYAAPAPEQAYGYGPYGGAYPPGTQVVYAANGQAYAVPYQYPYAGLYGQQPANQVIIRERYRDNDSDLALGMLAGAATGMALGSLFWVF |
| 预测分子量 | 25 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PLEKHB2重组蛋白的3篇代表性文献概览(文献名为虚构示例，仅供参考)：
1. **《PLEKHB2重组蛋白在细胞凋亡调控中的作用》**
- 作者：Smith A, et al.
- 摘要：本研究通过大肠杆菌表达系统成功纯化重组PLEKHB2蛋白，发现其通过结合磷脂酰肌醇信号通路抑制线粒体依赖性细胞凋亡，为癌症治疗提供潜在靶点。
2. **《重组PLEKHB2蛋白的结构与脂质结合特性分析》**
- 作者：Lee JH, et al.
- 摘要：利用X射线晶体学解析了PLEKHB2重组蛋白的PH结构域三维结构，揭示其特异性结合PI(3.4)P2脂质的分子机制，解释了其在细胞膜定位中的功能。
3. **《PLEKHB2重组蛋白促进乳腺癌细胞迁移的机制研究》**
- 作者：Zhang Y, et al.
- 摘要：在哺乳动物细胞中表达重组PLEKHB2蛋白，证实其通过激活Rho GTPase信号通路增强乳腺癌细胞迁移能力，提示其在肿瘤转移中的促进作用。
注：上述内容为模拟摘要，实际文献需通过PubMed/Google Scholar等平台以"PLEKHB2 recombinant protein"为关键词检索。
**Background of PLEKHB2 Recombinant Protein**
PLEKHB2 (Pleckstrin Homology Domain-Containing Protein B2) is a member of the pleckstrin homology (PH) domain-containing protein family, which plays roles in intracellular signaling, membrane trafficking, and cytoskeletal organization. The PH domain, a conserved structural motif, enables interactions with lipids or proteins, facilitating localization to cellular membranes or signal transduction complexes. PLEKHB2 is ubiquitously expressed, with notable presence in tissues like the brain, heart, and kidneys, though its precise biological functions remain under investigation.
Studies suggest PLEKHB2 may regulate cellular processes such as apoptosis, autophagy, and vesicle transport. For instance, it has been implicated in modulating mitochondrial dynamics and ER (endoplasmic reticulum) membrane remodeling, potentially through interactions with lipids or proteins involved in membrane curvature. Dysregulation of PLEKHB2 has been linked to pathological conditions, including cancer and neurodegenerative diseases. In certain cancers, elevated PLEKHB2 expression correlates with tumor progression and metastasis, possibly by promoting cell survival or invasiveness. Conversely, in neurodegenerative contexts, loss-of-function mutations or reduced expression might disrupt neuronal homeostasis.
Recombinant PLEKHB2 protein is engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for functional studies. It typically includes tags (e.g., His-tag) for purification and detection. Researchers utilize this protein to explore its structural properties, binding partners, and mechanistic roles *in vitro* or in cell-based assays. Its applications span elucidating molecular pathways, validating drug targets, or developing diagnostic tools.
Despite progress, many aspects of PLEKHB2’s biology—such as its exact interactome, context-dependent roles in disease, and therapeutic potential—require further exploration. The recombinant protein serves as a critical tool to address these questions, advancing both basic and translational research.
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