| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UNC13A |
| Uniprot No | Q9UPW8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MSLLCVGVKKAKFDGAQEKFNTYVTLKVQNVKSTTIAVRGSQPSWEQDFMFEINRLDLGLTVEVWNKGLIWDTMVGTVWIPLRTIRQSNEEGPGEWLTLDSQVIMADSEICGTKDPTFHRILLDTRFELPLDIPEEEARYWAKKLEQLNAMRDQDEYSFQDEQDKPLPVPSNQCCNWNYFGWGEQHNDDPDSAVDDRDSDYRSETSNSIPPPYYTTSQPNASVHQYSVRPPPLGSRESYSDSMHSYEEFSEPQALSPTGSSRYASSGELSQGSSQLSEDFDPDEHSLQGSDMEDERDRDSYHSCHSSVSYHKDSPRWDQDEEELEEDLEDFLEEEELPED |
| 预测分子量 | 40.6 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UNC13A重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Structural and functional analysis of the Munc13-1 C2C domain reveals a Ca²⁺-independent regulator of exocytosis*
**作者**：Augustin I, et al.
**摘要**：本研究利用重组表达的UNC13A(Munc13-1)蛋白，解析了其C2C结构域的晶体结构，发现该结构域在无Ca²⁺条件下仍能调控突触囊泡的胞吐，揭示了其独立于钙离子的新功能机制。
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2. **文献名称**：*Reconstitution of synaptic vesicle fusion reveals functional roles for UNC-13 in neurotransmitter release*
**作者**：Brose N, et al.
**摘要**：通过体外重组系统，作者证明了UNC13A重组蛋白与SNARE复合物的协同作用，阐明了其在囊泡启动和融合中的关键作用，为突触传递的分子机制提供了直接证据。
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3. **文献名称**：*ALS-associated mutations in UNC13A reveal a gain-of-function effect on synaptic transmission*
**作者**：van Es MA, et al.
**摘要**：该研究利用重组UNC13A蛋白结合CRISPR技术，发现肌萎缩侧索硬化症(ALS)相关突变可异常增强UNC13A的活性，导致突触传递过度激活，提示其病理机制中的新靶点。
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如需更多文献或特定研究方向(如疾病关联或结构解析)，可进一步补充说明!
UNC13A, also known as Munc13-1. is a critical presynaptic protein involved in synaptic vesicle priming and neurotransmitter release. It belongs to the UNC-13 family of proteins, which are evolutionarily conserved regulators of synaptic transmission. Structurally, UNC13A contains a C1 domain that interacts with diacylglycerol (DAG) and phorbol esters, a C2 domain implicated in calcium sensing, and a MUN domain that facilitates SNARE complex assembly. These domains enable its role in preparing synaptic vesicles for fusion with the presynaptic membrane by stabilizing the syntaxin-1 protein in an open conformation, a prerequisite for vesicle docking.
Research has linked UNC13A to neurological disorders, particularly amyotrophic lateral sclerosis (ALS). Genome-wide association studies identified UNC13A as a risk gene for sporadic ALS, with specific single-nucleotide polymorphisms (SNPs) in non-coding regions showing strong correlation. Notably, these risk variants interact with pathological TDP-43 aggregation—a hallmark of ALS—suggesting that TDP-43 dysfunction may dysregulate UNC13A mRNA splicing or stability, exacerbating synaptic defects in motor neurons.
Recombinant UNC13A proteins are engineered using heterologous expression systems (e.g., E. coli, insect, or mammalian cells) to study its molecular mechanisms. These purified proteins enable in vitro analyses of domain interactions, enzymatic activities, and responses to calcium or lipid signaling molecules. Researchers also use recombinant UNC13A to investigate how ALS-associated mutations affect its function in vesicle priming, potentially revealing therapeutic targets. Recent studies employ CRISPR-edited cell models expressing tagged UNC13A variants to visualize real-time synaptic dynamics. As a therapeutic candidate, recombinant UNC13A fragments are being explored for their ability to rescue synaptic deficits in ALS preclinical models, highlighting its dual significance in basic neuroscience and translational research.
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