| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPIN1 |
| Uniprot No | Q9Y657 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-262aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMKTPFGK TPGQRSRADA GHAGVSANMM KKRTSHKKHR SSVGPSKPVS QPRRNIVGCR IQHGWKEGNG PVTQWKGTVL DQVPVNPSLY LIKYDGFDCV YGLELNKDER VSALEVLPDR VATSRISDAH LADTMIGKAV EHMFETEDGS KDEWRGMVLA RAPVMNTWFY ITYEKDPVLY MYQLLDDYKE GDLRIMPDSN DSPPAEREPG EVVDSLVGKQ VEYAKEDGSK RTGMVIHQVE AKPSVYFIKF DDDFHIYVYD LVKTS |
| 预测分子量 | 32 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3篇关于SPIN1重组蛋白的相关文献摘要概括(虚构示例，仅作格式参考)：
1. **文献名称**: "Expression and purification of recombinant SPIN1 protein for structural studies"
**作者**: Zhang Y, et al.
**摘要**: 该研究利用大肠杆菌表达系统成功表达并纯化重组人源SPIN1蛋白，优化了诱导条件和层析步骤，获得高纯度蛋白用于后续X射线晶体结构解析，揭示了其Tudor结构域的RNA结合特性。
2. **文献名称**: "SPIN1 interacts with histone H3K4me3 to regulate gene transcription in cancer cells"
**作者**: Li H, et al.
**摘要**: 通过重组SPIN1蛋白的体外结合实验，证明其通过Tudor结构域特异性识别组蛋白H3K4三甲基化修饰，并在癌细胞中通过此互作调控下游致癌基因的转录活性。
3. **文献名称**: "Functional characterization of SPIN1 in mouse embryonic stem cells using recombinant protein delivery"
**作者**: Wang X, et al.
**摘要**: 研究采用重组SPIN1蛋白直接递送到小鼠胚胎干细胞中，发现其通过维持染色质开放状态促进多能性基因(如Oct4、Nanog)的表达，揭示了其在干细胞自我更新中的关键作用。
(注：以上文献为示例性质，实际引用需根据具体研究检索PubMed等数据库获取真实文献。)
**Background of SPIN1 Recombinant Protein**
SPIN1 (Spindlin1) is a chromatin-binding protein encoded by the *SPIN1* gene, belonging to the SPIN/SSTY protein family. It is characterized by tandem Tudor domains, which enable specific recognition of methylated histone marks, particularly H3K4me3 (trimethylated lysine 4 on histone H3). This interaction links SPIN1 to epigenetic regulation, influencing gene expression by modulating chromatin structure and transcriptional activity.
SPIN1 plays critical roles in early embryonic development, cell cycle progression, and stem cell maintenance. It is highly expressed in germ cells and certain cancers, where its dysregulation is associated with tumorigenesis. For instance, SPIN1 overexpression in cancers like hepatocellular carcinoma or ovarian cancer correlates with poor prognosis, likely due to its role in enhancing oncogenic signaling pathways such as Wnt/β-catenin.
Recombinant SPIN1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional and structural studies. Its purified form retains the ability to bind methylated histones and other partners, making it a valuable tool for investigating epigenetic mechanisms, protein-DNA/RNA interactions, and chromatin dynamics. Researchers also utilize SPIN1 recombinant protein to screen small-molecule inhibitors targeting its Tudor domains, aiming to develop therapies for SPIN1-driven cancers.
Structural studies of recombinant SPIN1. including X-ray crystallography and NMR, have revealed molecular details of its histone-binding specificity and conformational flexibility. These insights aid in understanding how SPIN1 integrates epigenetic signals to regulate cellular processes, highlighting its potential as a therapeutic or diagnostic target in diseases linked to epigenetic dysregulation.
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