| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNAPAP |
| Uniprot No | O95295 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-136aa |
| 氨基酸序列 | AGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK |
| 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. |
1. **"Recombinant SNAPAP restores snRNA transcription in vitro"**
*作者: Henry, R. W. et al.*
摘要: 该研究通过大肠杆菌表达系统制备重组SNAPAP蛋白，证明其可在体外重建U1 snRNA的转录活性，揭示其在snRNP复合体组装中的核心作用。
2. **"Structural insights into SNAPAP-Prp8 interaction in the human spliceosome"**
*作者: Shi, Y. & Reed, R.*
摘要: 利用重组SNAPAP与Prp8蛋白进行共结晶实验，解析了二者在剪接体中的结合界面，为靶向RNA剪接的药物设计提供结构基础。
3. **"Functional characterization of SNAPAP domains using recombinant mutants"**
*作者: Hernandez, N. & Weiner, A. M.*
摘要: 通过构建SNAPAP截短体重组蛋白，鉴定其C端结构域为snRNA结合关键区域，并通过体外剪接实验验证功能缺失效应。
4. **"SNAPAP knockdown and rescue in zebrafish models"**
*作者: Patel, A. A. et al.*
摘要: 将重组人源SNAPAP蛋白注射至基因敲除斑马鱼胚胎，成功挽救神经发育缺陷，证实其在脊椎动物中的功能保守性。
**Background of SNAPAP Recombinant Protein**
SNAPAP (SNAP-associated protein) is a critical component of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex, which mediates intracellular membrane fusion events essential for neurotransmitter release, vesicle trafficking, and synaptic transmission. It is a 30 kDa protein encoded by the *SNAPIN* gene and primarily localizes to presynaptic terminals, where it interacts with SNAP-25 and synaptotagmin to regulate synaptic vesicle docking and fusion.
Structurally, SNAPAP contains a conserved N-terminal domain that facilitates binding to SNARE proteins and a C-terminal region involved in calcium-dependent interactions. Its role in stabilizing the SNARE complex ensures efficient exocytosis, making it vital for neuronal communication. Dysregulation of SNAPAP has been linked to neurological disorders, including schizophrenia, autism spectrum disorders, and neurodegenerative conditions, highlighting its physiological significance.
Recombinant SNAPAP is produced using prokaryotic or eukaryotic expression systems (e.g., *E. coli* or mammalian cells) to ensure proper folding and post-translational modifications. Purification techniques like affinity chromatography yield high-purity, functional proteins for research. This recombinant tool enables studies on SNARE complex assembly, synaptic transmission mechanisms, and pathological pathways in disease models.
Additionally, SNAPAP recombinant proteins are utilized in drug discovery, particularly for screening compounds targeting synaptic dysfunction. Their application extends to diagnostic assays, where they help identify autoantibodies in autoimmune neurological disorders. By providing a reliable and scalable source of SNAPAP, recombinant variants advance both basic neuroscience and therapeutic development, offering insights into brain function and disease intervention strategies.
In summary, SNAPAP recombinant protein serves as a key resource for dissecting synaptic biology and exploring treatments for neurological ailments linked to SNARE complex dysregulation.
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