NLRC4 Antibodies

Structure of NLRC4

NLRC4 is an intracellular pattern recognition receptor protein with a molecular weight of approximately 110-116 kDa. Its exact molecular weight varies among different species, mainly due to minor changes in the protein domain structure.

This protein is composed of approximately 1024 amino acids and its tertiary structure exhibits a modular configuration: the N-terminal CARD domain is responsible for binding to downstream signaling molecules ASC; the central NACHT domain mediates self-oligomerization to form the platform of the inflammasome; the C-terminal LRR domain is responsible for recognizing ligands or maintaining the protein's self-inhibitory state. The activation mechanism of this protein depends on the assembly of its quaternary structure: when the LRR domain senses signals from bacterial flagellin protein or components of the type III secretion system, the NACHT domain undergoes a conformational change, driving multiple NLRC4 monomers to aggregate through homotypic interactions into a disc-shaped supercomplex (inflammasome), thereby recruiting and activating caspase-1.

Fig. 1 Protein domain structure of NLRC4.¹

Key structural properties of NLRC4:

• Modular multi-domain configuration
• Combining with ATP hydrolysis activity NACHT structure domain
• The C-terminal LRR domain maintains the autoinhibitory state of the protein by interacting with the NACHT domain in the resting state
• Key histidine residues located in the NACHT domain are critical for sensing activation signals and triggering conformation rearrangements

Functions of NLRC4

The main function of NLRC4 is to act as an intracellular immune receptor, recognizing pathogenic signals and assembling inflammasomes. However, it is also involved in various physiological and pathological processes such as regulating pyroptosis and maintaining immune homeostasis.

Unlike immune receptor complexes that rely on multiple subunits for collaboration, the activation of NLRC4 exhibits a nearly "switch-like" rapid oligomerization feature. This dramatic conformational transition from the inactive self-inhibitory state to the active oligomerized state ensures a rapid and strong response to pathogen invasion.

Applications of NLRC4 and NLRC4 Antibody in Literature

1. Wen, Jiexia, et al. "Updating the NLRC4 inflammasome: from bacterial infections to autoimmunity and cancer." Frontiers in immunology 12 (2021): 702527. https://doi.org/10.3389/fimmu.2021.702527

The article indicates that the NLRC4 inflammasome is an intracellular multi-protein complex that can recognize pathogenic signals and activate caspase-1, promoting the maturation and release of IL-1β and IL-18. It plays an important regulatory role in anti-infection, autoimmune diseases, and cancer. This article reviews its composition, activation mechanism, and disease association.

2. Guan, Chenyang, et al. "SIRT3-mediated deacetylation of NLRC4 promotes inflammasome activation." Theranostics 11.8 (2021): 3981. https://doi.org/10.7150/thno.55573

The article indicates that SIRT3 mediates the deacetylation of Lys71 and Lys272 sites of the NLRC4 protein, thereby promoting the assembly and activation of the NLRC4 inflammasome, and enhancing the inflammatory response and cell pyroptosis of macrophages in resisting Salmonella infection.

3. Chen, Hui, et al. "NLRP12 collaborates with NLRP3 and NLRC4 to promote pyroptosis inducing ganglion cell death of acute glaucoma." Molecular Neurodegeneration 15.1 (2020): 26. https://doi.org/10.1186/s13024-020-00372-w

This study reveals that in acute glaucoma, microglia activate the NLRP12/NLRP3/NLRC4 inflammasome through the CASP8-HIF-1α axis, mediate GSDMD-dependent pyroptosis of retinal ganglion cells, and cause the amplification of neuroinflammation cascade.

4. Steiner, Annemarie, et al. "Recessive NLRC4-autoinflammatory disease reveals an ulcerative colitis locus." Journal of clinical immunology 42.2 (2022): 325-335. https://doi.org/10.1007/s10875-021-01175-4

This study is the first to discover that the homozygous mutation p.A160T of the NLRC4 gene can cause hereditary autoinflammatory diseases, and it has been confirmed in vitro that this mutation enhances the activation of the inflammasome. The heterozygous mutant significantly increases the risk of developing ulcerative colitis.

5. Lage, Silvia Lucena, et al. "Emerging concepts about NAIP/NLRC4 inflammasomes." Frontiers in immunology 5 (2014): 309. https://doi.org/10.3389/fimmu.2014.00309

The article indicates that the NAIP/NLRC4 inflammasome can recognize bacterial flagella, needle-like and rod-like proteins and other components. It activates caspase-1 to mediate the maturation of IL-1β/IL-18 and cell pyroptosis, and participates in various immune regulatory processes. It plays a crucial role in anti-infection and tumor immunity.

Creative Biolabs: NLRC4 Antibodies for Research

Creative Biolabs specializes in the production of high-quality NLRC4 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom NLRC4 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our NLRC4 antibodies, custom preparations, or technical support, contact us at email.