| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NLRP3 |
| Uniprot No | Q96P20 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 733-1036aa |
| 氨基酸序列 | LFSVLSTSQSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVVFEPSW |
| 预测分子量 | 40.7 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NLRP3重组蛋白的3篇代表性文献(简化格式)：
1. **标题**：*Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome*
**作者**：Shi Y. et al.
**摘要**：通过冷冻电镜解析了重组人源NLRP3蛋白与接头蛋白NEK7的复合物结构，揭示了NEK7介导的NLRP3寡聚化及炎症小体激活的分子机制。
2. **标题**：*Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation*
**作者**：Faustin B. et al.
**摘要**：体外重组NALP3(NLRP3)炎症小体复合物，证明其通过ATP水解依赖的寡聚化触发caspase-1活化，并验证了疾病相关突变对活性的影响。
3. **标题**：*Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization*
**作者**：Zhang L. et al.
**摘要**：利用重组蛋白系统解析了NAIP-NLRC4炎症小体的激活机制，为NLR家族蛋白(含NLRP3)的寡聚模式提供了结构生物学参考。
(注：以上内容为示例，实际文献需根据具体研究补充，建议通过PubMed/Google Scholar以"NLRP3 recombinant protein"为关键词检索近年高被引论文。)
NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) is a critical component of the innate immune system, functioning as a cytosolic pattern recognition receptor. It belongs to the NOD-like receptor (NLR) family and plays a central role in assembling the NLRP3 inflammasome, a multiprotein complex that activates inflammatory responses. Structurally, NLRP3 consists of three domains: an N-terminal pyrin domain (PYD) for protein-protein interactions, a central NACHT domain with ATPase activity for oligomerization, and a C-terminal leucine-rich repeat (LRR) domain implicated in ligand sensing and autoinhibition.
The NLRP3 inflammasome is activated by diverse stimuli, including pathogen-associated molecular patterns (PAMPs), damage-associated molecular patterns (DAMPs), and cellular stress signals (e.g., reactive oxygen species, ion flux). Upon activation, NLRP3 recruits the adaptor protein ASC and procaspase-1. triggering caspase-1-mediated cleavage of pro-inflammatory cytokines IL-1β and IL-18 into their active forms. This process also induces pyroptosis, a lytic cell death that amplifies inflammation.
Dysregulated NLRP3 activity is linked to numerous diseases, such as Alzheimer’s, atherosclerosis, gout, and autoimmune disorders. Recombinant NLRP3 proteins, produced via heterologous expression systems (e.g., E. coli, mammalian cells), are essential tools for studying inflammasome mechanisms, screening inhibitors, and developing therapeutics. For instance, recombinant NLRP3 enables structural studies (e.g., cryo-EM) to elucidate activation mechanisms and facilitates high-throughput drug discovery targeting NLRP3-driven pathologies. Current research focuses on designing NLRP3-specific inhibitors (e.g., MCC950) to mitigate chronic inflammation while preserving essential immune functions.
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