| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPI1 |
| Uniprot No | P17947 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-270aa |
| 氨基酸序列 | MLQACKMEGFPLVPPPSEDLVPYDTDLYQRQTHEYYPYLSSDGESHSDHYWDFHPHHVHSEFESFAENNFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHPSLGHQVSYLPRMCLQYPSLSPAQPSSDEEEGERQSPPLEVSDGEADGLEPGPGLLPGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRHPPH |
| 预测分子量 | 35.1kDa |
| 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SPI1(PU.1)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural and functional analysis of the PU.1 protein through recombinant expression in E. coli*
**作者**：Smith J, et al.
**摘要**：本研究报道了在大肠杆菌中高效表达并纯化重组SPI1(PU.1)蛋白的方法，通过X射线晶体学解析其DNA结合域的三维结构，揭示了其特异性识别靶基因启动子的分子机制。
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2. **文献名称**：*Recombinant PU.1 regulates myeloid differentiation in hematopoietic stem cells*
**作者**：Li Y, et al.
**摘要**：利用哺乳动物细胞表达系统制备功能性重组SPI1蛋白，证明其通过调控下游基因(如CSF1R)的表达，促进髓系祖细胞向巨噬细胞分化，为白血病治疗提供潜在靶点。
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3. **文献名称**：*Development of a SPI1 recombinant protein-based assay for screening transcriptional inhibitors*
**作者**：Garcia R, et al.
**摘要**：构建重组SPI1蛋白的高通量筛选平台，用于鉴定抑制其与DNA结合的化合物，发现小分子抑制剂可阻断PU.1在淋巴瘤细胞中的促癌活性，为药物开发提供新策略。
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注：以上文献信息为示例性概括，实际文献需通过数据库(如PubMed、Web of Science)检索确认。若需具体文献，建议使用关键词“PU.1 recombinant protein”或“SPI1 expression”进一步查询。
SPI1 (also known as PU.1) is a member of the ETS family of transcription factors, playing a critical role in hematopoietic development and immune cell differentiation. Encoded by the *SPI1* gene, this protein regulates the expression of genes involved in myeloid and B-cell lineage commitment by binding to purine-rich DNA sequences via its conserved ETS domain. Its function is essential for the maturation of monocytes, macrophages, neutrophils, and B lymphocytes, with knockout studies in mice demonstrating lethal defects in hematopoiesis.
Recombinant SPI1 protein is engineered through molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems to ensure proper post-translational modifications. The purified protein retains its DNA-binding activity and transcriptional regulatory properties, making it valuable for *in vitro* studies. Researchers utilize recombinant SPI1 to investigate mechanisms of hematologic malignancies, as dysregulated SPI1 expression is linked to acute myeloid leukemia (AML) and other blood disorders. It also serves as a tool for probing immune cell differentiation pathways, chromatin immunoprecipitation (ChIP) assays, and screening therapeutic compounds targeting SPI1-dependent oncogenic pathways.
Structurally, SPI1 contains an N-terminal transactivation domain and a C-terminal ETS domain. Mutagenesis studies on recombinant variants have elucidated residues critical for DNA interaction and protein stability. Recent advancements in cryo-EM and X-ray crystallography using recombinant SPI1 have further resolved its binding dynamics with cofactors like IRF4/8 in gene regulation. Its role in autoimmune diseases and infection responses remains an active research area, underscoring its broad biomedical relevance. Commercial recombinant SPI1 products often include tags (e.g., His, GST) for simplified purification and detection in experimental workflows.
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