纯度 | >85 % SDS-PAGE. |
种属 | Human |
靶点 | CBFB |
Uniprot No | Q13951 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-182aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMPRVVPDQRSKFENEEFFRKLSRECEIKYT GFRDRPHEERQARFQNACRDGRSEIAFVATGTNLSLQFFPASWQGEQRQT PSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLDGMGCLEFDEE RAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEVRVSQLLAVTGKKTT RP |
预测分子量 | 24 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CBFB重组蛋白的3篇代表性文献的简要信息(注:文献为假设示例,实际需根据具体研究检索):
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1. **文献名称**: *Structural basis for the heterodimeric interaction between AML1/RUNX1 and CBFβ*
**作者**: Huang G, et al.
**摘要**: 本研究通过X射线晶体学解析了AML1/RUNX1与CBFβ重组蛋白的复合物结构,揭示了CBFβ通过稳定RUNX1的构象增强其DNA结合能力,为白血病相关突变机制提供了结构生物学依据。
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2. **文献名称**: *Functional rescue of CBFB-MYH11 fusion protein in leukemia cells by engineered recombinant CBFβ*
**作者**: Wang Q, et al.
**摘要**: 研究利用重组CBFβ蛋白在体外模型中逆转由CBFB-MYH11融合蛋白引起的造血分化阻滞,证明靶向CBFβ/RUNX1相互作用可能成为急性髓系白血病(AML)的治疗策略。
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3. **文献名称**: *High-yield purification and characterization of recombinant CBFβ for chromatin remodeling studies*
**作者**: Smith JL, et al.
**摘要**: 该文献报道了一种高效重组CBFβ蛋白的原核表达与纯化方法,优化了蛋白溶解度及稳定性,并验证其在体外染色质重塑复合体组装中的功能活性。
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如需具体文献,建议通过PubMed或Web of Science以“CBFB recombinant protein”、“CBFβ-RUNX complex”为关键词检索近年研究。
CBFB (Core Binding Factor Subunit Beta) is a critical regulatory protein that plays a central role in hematopoietic development, cell differentiation, and transcriptional regulation. It functions by forming a heterodimeric complex with members of the RUNX family (RUNX1. RUNX2. RUNX3), enhancing their DNA-binding affinity and stability. This CBFB-RUNX interaction is essential for regulating genes involved in blood cell formation, skeletal morphogenesis, and immune responses. Structurally, CBFB contains an evolutionarily conserved N-terminal domain responsible for RUNX binding and a C-terminal domain implicated in modulating transcriptional activity.
The recombinant CBFB protein, produced via genetic engineering in systems like *E. coli* or mammalian cells, enables detailed mechanistic studies of these interactions. Researchers often engineer tags (e.g., His, FLAG) into recombinant CBFB to facilitate purification and detection. Its applications span structural biology (e.g., crystallography of CBFB-RUNX-DNA complexes), functional assays (e.g., chromatin immunoprecipitation, luciferase reporter systems), and disease modeling, particularly in hematological malignancies. Notably, chromosomal translocations involving *CBFB* (e.g., CBFB-MYH11 in acute myeloid leukemia) generate oncogenic fusion proteins, making recombinant CBFB variants valuable tools for studying leukemogenesis and screening therapeutic agents. Additionally, it aids in exploring CBFB’s non-canonical roles, such as modulating oxidative stress responses. The development of recombinant CBFB has significantly advanced both basic research and translational studies in hematopoiesis and cancer biology.
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