| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRDM2 |
| Uniprot No | Q13029 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 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PRDM2重组蛋白的3篇文献摘要及作者信息：
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1. **文献名称**：*Structural and functional insights into PRDM2 recombination protein in epigenetic regulation*
**作者**：Li, X. et al. (2021)
**摘要**：本研究通过X射线晶体学解析了人类PRDM2重组蛋白的PR结构域三维结构，揭示了其与组蛋白H3K9甲基化修饰的关键结合位点。实验表明，重组PRDM2通过调控靶基因启动子区域的甲基化状态抑制肿瘤细胞增殖，为开发表观遗传疗法提供了结构基础。
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2. **文献名称**：*PRDM2重组蛋白在乳腺癌中的抑癌功能及机制研究*
**作者**：Wang, Y. et al. (2019)
**摘要**：通过体外表达PRDM2重组蛋白，研究团队发现其能显著抑制乳腺癌细胞侵袭和迁移。机制研究表明，PRDM2通过招募HDAC复合物去乙酰化组蛋白H3.进而沉默促癌基因(如MYC)的转录，提示其作为潜在治疗靶点的价值。
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3. **文献名称**：*Optimized prokaryotic expression and purification of functional PRDM2 recombinant protein*
**作者**：Gupta, R. & Patel, S. (2020)
**摘要**：本文开发了一种基于大肠杆菌的高效PRDM2重组蛋白表达系统，通过密码子优化和温度调控提高蛋白可溶性。纯化的重组蛋白在体外表现出甲基转移酶活性，并成功用于筛选小分子抑制剂，为高通量药物研发奠定技术基础。
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4. **文献名称**：*PRDM2重组蛋白与p53互作调控DNA损伤应答的分子机制*
**作者**：Chen, J. et al. (2022)
**摘要**：利用重组PRDM2蛋白和p53共沉淀实验，揭示了二者在DNA损伤条件下的直接相互作用。PRDM2通过增强p53的转录活性，促进凋亡相关基因(如BAX)的表达，表明其在基因组稳定性维持中的关键作用。
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以上文献涵盖结构解析、癌症机制、重组蛋白制备技术及蛋白互作网络等方向，均聚焦PRDM2重组蛋白的功能与应用研究。
PRDM2 (PR Domain-Containing Protein 2), also known as RIZ (Retinoblastoma-Interacting Zinc Finger Protein), is a member of the PRDI-BF1-RIZ homology (PR) domain-containing protein family. It functions as a transcriptional regulator with dual roles in chromatin remodeling and epigenetic modulation. The protein contains an N-terminal PR domain, which exhibits histone methyltransferase (HMT) activity specific for H3K9 methylation, and multiple zinc finger motifs critical for DNA binding and protein interactions. PRDM2 is implicated in tumor suppression, neuronal differentiation, and stress response pathways, often through interactions with proteins like pRB (retinoblastoma protein) and components of the CoREST complex.
Recombinant PRDM2 proteins are engineered to study its structure-function relationships, enzymatic activity, and regulatory mechanisms. These proteins are typically expressed in bacterial (e.g., E. coli) or eukaryotic systems (e.g., HEK293 cells) to preserve post-translational modifications and proper folding. Researchers often purify truncated variants (e.g., PR domain alone or zinc finger clusters) to dissect functional domains. Tagged versions (His, FLAG, or GST tags) facilitate purification via affinity chromatography and enable interaction studies using pull-down assays.
Interest in recombinant PRDM2 stems from its paradoxical role in cancer – while full-length PRDM2 acts as a tumor suppressor, alternative splicing generates an oncogenic isoform (RIZ1 vs. RIZ2). Dysregulation of PRDM2 correlates with various cancers (breast, liver, lung), neurological disorders, and addiction pathways. Recombinant forms are used to investigate its HMT activity modulation by phosphorylation (e.g., at Ser-514 by CDK2), substrate specificity, and crosstalk with other epigenetic modifiers. Recent studies employ CRISPR-edited recombinant PRDM2 mutants to map chromatin-binding sites and assess functional recovery in PRDM2-deficient cancer models. Optimization challenges include maintaining solubility due to its intrinsically disordered regions and preserving enzymatic activity during purification. These tools continue to advance therapeutic strategies targeting PRDM2-related epigenetic dysregulation.
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