| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | add |
| Uniprot No | P22333 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-333aa |
| 氨基酸序列 | MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIEDAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPGVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRALREKVAAK |
| 预测分子量 | 52.4 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. |
以下是关于重组蛋白(以ADD结构域相关研究为例)的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L (ADD) domain*
**作者**：Jia, D., Jurkowska, R.Z., Zhang, X. 等
**摘要**：该研究解析了DNMT3A的ADD结构域与未甲基化组蛋白H3K4结合的晶体结构，揭示了ADD结构域通过识别H3K4me0抑制DNA甲基转移酶活性的分子机制，为表观遗传调控提供结构基础。
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2. **文献名称**：*The ATRX-ADD domain binds to H3K9me3-containing nucleosomes to suppress chromatin remodeling*
**作者**：Eustermann, S., Yang, J.C., Law, M.J. 等
**摘要**：通过体外重组实验和冷冻电镜技术，阐明了ATRX蛋白的ADD结构域特异性结合H3K9me3修饰的核小体，进而抑制染色质重塑复合物活性，在端粒异染色质维持中发挥关键作用。
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3. **文献名称**：*Recombinant production of SUMO-tagged ADD domain proteins for structural and functional studies*
**作者**：Marblestone, J.G., Edavettal, S.C., Lim, Y. 等
**摘要**：开发了一种基于SUMO融合标签的重组蛋白表达系统，用于高效可溶表达ADD结构域蛋白(如DNMT3L)，并通过亲和层析一步纯化，显著提高蛋白产量和稳定性，适用于结构生物学研究。
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**注**：ADD结构域(ATRX-DNMT3-DNMT3L结构域)在表观遗传调控中广泛参与组蛋白修饰识别与酶活性调控。以上文献聚焦其结构、功能及重组表达技术，涵盖基础机制与应用方法。
**Background of ADD Recombinant Proteins**
ADD (ATRX-DNMT3-DNMT3L) recombinant proteins are engineered constructs derived from the conserved ADD domain, a zinc-binding motif found in chromatin-associated proteins like ATRX (Alpha-Thalassemia/Mental Retardia Syndrome X-linked), DNMT3A/DNMT3B (DNA methyltransferases), and DNMT3L. This domain plays a critical role in mediating interactions between these proteins and histone post-translational modifications, particularly H3K4me0 (unmethylated histone H3 lysine 4), facilitating site-specific DNA methylation and chromatin remodeling.
The ADD domain’s structural and functional significance lies in its ability to act as a molecular bridge, linking epigenetic modifiers to specific genomic regions. Dysregulation of ADD-containing proteins is implicated in developmental disorders (e.g., ATRX syndrome), cancers, and imprinting diseases. Recombinant ADD proteins are generated via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study these interactions *in vitro* or for therapeutic screening.
By isolating the ADD domain, researchers analyze its binding specificity, conformational dynamics, and role in recruiting enzymatic partners. Such studies enhance understanding of epigenetic regulation and aid in designing inhibitors targeting aberrant DNA methylation in diseases. The use of recombinant ADD proteins also supports structural biology efforts, including X-ray crystallography and NMR, to resolve mechanisms underlying chromatin interaction and disease-associated mutations.
Overall, ADD recombinant proteins serve as vital tools for dissecting the molecular basis of epigenetic signaling and advancing therapeutic strategies for related pathologies.
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