NAIP抗体

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     The image is immunohistochemistry of paraffin-embedded Human thyroid cancer tissue using P05078(NAIP Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human brain  tissue using P05078(NAIP Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

NAIP (NLR family apoptosis inhibitory protein) is a member of the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family, which plays a critical role in innate immunity. It functions as an intracellular sensor for bacterial pathogens by recognizing specific microbial components. Structurally, NAIP contains a central NACHT domain for nucleotide binding and oligomerization, along with C-terminal leucine-rich repeats (LRRs) involved in ligand recognition.

In humans, a single NAIP gene exists, while mice possess multiple paralogs (Naip1-6) with distinct pathogen specificities. NAIP proteins detect bacterial flagellin or components of type III secretion systems (e.g., PrgJ, BsaK) from pathogens like *Salmonella* or *Legionella*. Upon ligand binding, NAIP recruits NLRC4 to form the inflammasome complex, triggering caspase-1 activation, pyroptosis, and IL-1β/IL-18 release.

NAIP antibodies are essential tools for studying inflammasome activation, protein localization, and host-pathogen interactions. Dysregulation of NAIP has been linked to diseases, including spinal muscular atrophy (SMA) due to genomic proximity to the *SMN1* gene, and inflammatory disorders. Research also explores NAIP’s role in cancer and neurodegenerative diseases. Therapeutic strategies targeting NAIP-NLRC4 signaling aim to modulate excessive inflammation or enhance pathogen clearance.