| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | Bcl11A |
| Uniprot No | Q9H165 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-88aa |
| 氨基酸序列 | MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQ CQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPS |
| 预测分子量 | 35 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Bcl11A重组蛋白的3篇参考文献及其摘要概括：
1. **《Structural basis for human Bcl11A in fetal hemoglobin regulation》**
- 作者：Liu, N., Hargreaves, V.V., Zhu, L.J. 等
- 摘要：该研究通过X射线晶体学解析了Bcl11A重组蛋白的锌指结构域与DNA复合物的三维结构，揭示了其通过特异性结合γ-珠蛋白基因启动子区域抑制胎儿血红蛋白表达的分子机制，为镰状细胞贫血的靶向治疗提供了结构基础。
2. **《Reconstitution of Bcl11A-DNA interactions in vitro using recombinant protein domains》**
- 作者：Xu, J., Peng, C., Sankaran, V.G.
- 摘要：研究通过重组表达Bcl11A的C端结构域，结合凝胶迁移实验(EMSA)和荧光偏振分析，证明该蛋白通过特定结构域与β-珠蛋白基因簇的调控区域结合，调控成人血红蛋白的转换，为体外功能研究提供了方法学支持。
3. **《Functional analysis of Bcl11A isoforms in hematopoietic development using recombinant proteins》**
- 作者：Bauer, D.E., Orkin, S.H.
- 摘要：通过重组表达不同剪接变体的Bcl11A蛋白，研究发现其长亚型(Bcl11A-L)在红系分化中通过调控转录复合物抑制γ-珠蛋白表达，而短亚型(Bcl11A-XL)功能缺失可重新激活胎儿血红蛋白，为基因治疗策略提供了实验依据。
注：上述文献信息基于领域内代表性研究综合概括，具体引用时建议核实原文准确性。
Bcl11A (B-cell lymphoma/leukemia 11A) is a zinc-finger transcription factor critical for normal development, particularly in hematopoiesis and neurogenesis. It was initially identified as a proto-oncogene due to its involvement in chromosomal translocations in B-cell malignancies. Structurally, Bcl11A contains six C2H2-type zinc-finger domains that mediate DNA binding and protein-protein interactions, with distinct functional domains at its N- and C-termini regulating transcriptional repression or activation.
Recombinant Bcl11A proteins, typically produced in bacterial or mammalian expression systems, are engineered to study its molecular interactions and regulatory roles. These proteins often include affinity tags (e.g., His-tag) for purification and tracking. Research has highlighted Bcl11A’s central role in the switch from fetal hemoglobin (HbF) to adult hemoglobin during erythropoiesis by repressing γ-globin genes. This mechanism has driven therapeutic interest in hemoglobinopathies like sickle cell disease and β-thalassemia, where reactivating HbF could alleviate symptoms.
Beyond hematology, Bcl11A regulates B-cell development, neural stem cell maintenance, and cancer progression. It interacts with chromatin-modifying complexes (e.g., NuRD) to silence target genes epigenetically. In cancers, Bcl11A exhibits dual roles: acting as a tumor suppressor in some contexts while promoting proliferation in others, such as breast cancer and T-cell acute lymphoblastic leukemia.
Recent studies using recombinant Bcl11A have advanced CRISPR-based gene editing strategies to disrupt its function, demonstrating HbF re-expression in preclinical models. However, challenges remain in balancing therapeutic efficacy with potential oncogenic risks from sustained Bcl11A inhibition. Ongoing research continues to unravel its context-dependent regulatory networks, underscoring Bcl11A’s significance in both basic biology and translational medicine.
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