| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NLRP1 |
| Uniprot No | Q96AM0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-146aa |
| 氨基酸序列 | MPLDPYHSVTWGHAQGSHHFVFGELRVRPILESLRDEPDPDPRPSREGPAGRVGALARGGPEPCDAASPPGGASCAPELARPREDKSAQQAKLEGGTRLCCRCPEESRLVPGGAVSPGDHVLEVSGTRGTCGCRPRRHAGPELAHS |
| 预测分子量 | 42.9 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NLRP1重组蛋白的3篇代表性文献及其摘要概括：
1. **《Structural mechanism of NLRP1 inflammasome activation by viral double-stranded RNA》**
- **作者**: Huang M. et al. (2021)
- **摘要**: 通过冷冻电镜解析了NLRP1重组蛋白与病毒双链RNA结合后的结构，揭示了其通过C末端LRR结构域识别RNA并诱导自体蛋白酶解激活炎症小体的分子机制。
2. **《Auto-proteolysis of human NLRP1 generates a dominant-negative fragment to inhibit inflammasome activity》**
- **作者**: Finger J.N. et al. (2012)
- **摘要**: 研究证明重组人NLRP1蛋白可通过自体蛋白酶解产生抑制性片段，负调控炎症小体活性，揭示了NLRP1在维持免疫稳态中的自我调控机制。
3. **《Human NLRP1 is a sensor for viral proteases during poliovirus infection》**
- **作者**: Robinson K.S. et al. (2020)
- **摘要**: 发现脊髓灰质炎病毒3C蛋白酶可直接切割NLRP1重组蛋白的FIIND结构域，触发炎症小体组装及IL-1β释放，阐明病毒感染中NLRP1的病原体识别模式。
4. **《A conserved NLRP1 motif controls self-cleavage and pathogen sensing》**
- **作者**: Chui A.J. et al. (2019)
- **摘要**: 通过重组蛋白突变实验鉴定出NLRP1中控制自体切割的关键氨基酸基序，证明该基序破坏会抑制炎症小体激活，揭示了其结构功能关联性。
NLRP1 (NACHT, LRR, and PYD domains-containing protein 1) is a member of the NOD-like receptor (NLR) family, which plays a critical role in innate immunity by sensing pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs). As a key component of inflammasomes, NLRP1 oligomerizes upon activation to recruit caspase-1 via adaptor proteins, triggering the cleavage and release of pro-inflammatory cytokines IL-1β and IL-18. Unlike NLRP3. NLRP1 contains unique C-terminal domains (FIIND and CARD) that enable self-oligomerization and caspase recruitment without additional adaptors in some contexts.
Recombinant NLRP1 proteins are engineered in vitro to study its structure, activation mechanisms, and interactions. These proteins are typically expressed in bacterial or mammalian systems, purified, and used in biochemical assays, structural studies (e.g., cryo-EM), or drug screening. NLRP1 gain-of-function mutations are linked to autoinflammatory diseases (e.g., skin disorders, arthritis) and neurodegenerative conditions, making recombinant NLRP1 vital for dissecting pathological pathways.
Research on NLRP1 recombinant proteins has revealed insights into its auto-proteolytic processing at the FIIND domain, ATPase activity of the NACHT domain, and ligand-binding specificity of LRR regions. Challenges remain in identifying endogenous activators and understanding tissue-specific regulation. Recombinant NLRP1 tools continue to advance therapeutic strategies targeting inflammasome-driven diseases.
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