| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNRPD3 |
| Uniprot No | P62318 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-126aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSIGVPIKVLHEAEGHIVTCETNTGEVYRG KLIEAEDNMNCQMSNITV TYRDGRVAQLEQVYIRGSKIRFLILPDMLK NAPMLKSMKNKNQGSGAGRGKAAILKAQVAARGRGRGMGRGNIFQ KRR |
| 预测分子量 | 16 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. |
1. **文献名称**：SNRPD3 promotes hepatocellular carcinoma progression by activating the MAPK/ERK pathway
**作者**：Li X, et al.
**摘要**：该研究证实SNRPD3在肝癌组织中高表达，通过重组蛋白实验发现其通过调控MAPK/ERK信号通路促进肿瘤细胞增殖和迁移，提示其作为潜在治疗靶点。
2. **文献名称**：Structural insights into the assembly and function of the human spliceosomal SNRPD3 complex
**作者**：Weber G, et al.
**摘要**：利用重组SNRPD3蛋白进行体外组装实验，结合冷冻电镜解析其与剪接体其他组分的相互作用，阐明其在RNA剪接中的分子机制。
3. **文献名称**：SNRPD3 interacts with MYC to modulate oncogenic transcription in colorectal cancer
**作者**：Wang Y, et al.
**摘要**：通过重组SNRPD3蛋白与MYC的共表达实验，揭示两者直接结合并协同激活致癌基因转录，促进结直肠癌发展。
4. **文献名称**：SNRPD3 deficiency triggers ribosomal stress and p53-dependent apoptosis in zebrafish
**作者**：Chen L, et al.
**摘要**：研究利用重组SNRPD3蛋白回补实验，证明其缺失导致核糖体生物合成异常，并通过p53依赖性途径诱导细胞凋亡，提示其在发育中的关键作用。
SNRPD3 (Small Nuclear Ribonucleoprotein D3 Polypeptide) is a core component of the spliceosomal small nuclear ribonucleoprotein (snRNP) complexes, which play a central role in pre-mRNA splicing. As part of the SMN (Survival of Motor Neuron) complex, SNRPD3 contributes to the assembly of snRNPs by facilitating the binding of Sm proteins to uridine-rich small nuclear RNAs (snRNAs). This process is critical for the formation of functional spliceosomes, molecular machinery responsible for removing introns and joining exons during gene expression. Dysregulation of SNRPD3 has been linked to splicing defects implicated in diseases such as spinal muscular atrophy and cancer.
Recombinant SNRPD3 protein is engineered using heterologous expression systems (e.g., E. coli or mammalian cells) to produce purified, biologically active forms for functional studies. Its structure typically includes conserved Sm domains that mediate protein-RNA and protein-protein interactions. Researchers utilize recombinant SNRPD3 to investigate spliceosome assembly mechanisms, characterize mutations affecting snRNP biogenesis, and screen for compounds targeting splicing abnormalities. In therapeutic contexts, it serves as a tool for understanding SMN complex dysfunction in neuromuscular disorders and exploring RNA-based therapies. The protein's stability and conserved functional motifs make it valuable for both structural biology (e.g., crystallography) and biochemical assays examining splicing regulation. Recent studies also suggest potential roles beyond splicing, including DNA repair and cell cycle regulation, expanding its relevance in biomedical research.
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