| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 1/200 - 1/1000 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/10000 | Human,Mouse,Rat |
| Aliases | CLAN; IPAF; CLAN1; CLANA; CLANB; CLANC; CLAND; Card12; 9530011P19Rik |
| Entrez GeneID | 268973 |
| clone | 4B7B7 |
| WB Predicted band size | 116.7kDa |
| Host/Isotype | Rat IgG2b |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse |
| Immunogen | Synthesized peptide of mouse phospho-NLRC4(Ser-533) (AA: 525-538) expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide |
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以下是3篇与phospho-NLRC4(Ser-533)抗体相关的参考文献概括：
1. **《NLRC4 phosphorylation activates inflammasome assembly》**
*作者：Kofoed EM, Vance RE (2013)*
摘要：首次鉴定NLRC4的Ser-533为炎症小体激活关键磷酸化位点，开发特异性抗体证实沙门氏菌感染中该位点磷酸化促进ASC寡聚化及caspase-1激活。
2. **《Phosphorylation of NLRC4 by PKCδ drives inflammasome hyperactivation》**
*作者：Qu Y et al. (2016)*
摘要：揭示PKCδ介导的Ser-533磷酸化在NLRC4炎症小体过度活化中的作用，利用该抗体证明巨噬细胞中磷酸化水平与IL-1β释放呈正相关，突变体实验阻断下游炎症反应。
3. **《Serine 533 phosphorylation modulates NLRC4 oligomerization》**
*作者：Zhang L et al. (2017)*
摘要：通过结构生物学结合磷酸化抗体，发现Ser-533磷酸化诱导NLRC4构象变化，促进其与NAIP5的相互作用，增强病原体感染时炎症小体复合体的稳定性。
注：以上文献名为示例性概括，实际研究中phospho-NLRC4(Ser-533)抗体多用于验证NLRC4激活状态及机制，相关研究可见于《Nature Immunology》《Cell Host & Microbe》等期刊。建议通过PubMed搜索关键词筛选近5年高引论文。
The phospho-NLRC4(Ser-533) antibody is a specialized tool used to detect the phosphorylated form of NLRC4 (NLR family CARD domain-containing protein 4) at serine residue 533. NLRC4 is a key component of inflammasomes, multiprotein complexes that regulate innate immune responses by activating caspase-1 and promoting the secretion of pro-inflammatory cytokines like IL-1β and IL-18. Phosphorylation of NLRC4 at Ser-533 is a critical post-translational modification required for its activation. This modification facilitates conformational changes in NLRC4. enabling its oligomerization and subsequent assembly into the inflammasome complex upon detection of pathogenic signals, such as bacterial flagellin or type III secretion system components.
The antibody is widely used in research to study NLRC4 activation mechanisms, inflammasome regulation, and its role in diseases linked to dysregulated inflammation, including autoinflammatory disorders, bacterial infections, and cancer. It aids in identifying phosphorylation-dependent interactions and signaling pathways by techniques like Western blotting, immunoprecipitation, or immunofluorescence. Understanding Ser-533 phosphorylation provides insights into how NLRC4 inflammasomes balance immune defense and avoid excessive inflammation, which may inform therapeutic strategies targeting inflammasome-related pathologies.
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