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anti-Rat (Rattus) NLRP12 Antibodies:
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Human Polyclonal NLRP12 Primary Antibody for IHC (p), WB - ABIN657935
Cai, Batra, Del Piero, Jeyaseelan: NLRP12 modulates host defense through IL-17A-CXCL1 axis. in Mucosal immunology 2015
The obesity in humans correlates with reduced expression of adipose tissue NLRP12.
In a cohort of Vietnam War veterans (n = 299) NLRP12 polymorphisms were analysed for association with depression and coronary calcium scores. The NLRP12 polymorphism, rs34436714 was associated with a higher DASS21 Score for depression (p = 0.037). NLRP12 polymorphisms rs34971363 and rs6509825 (p = 0.022 and p = 0.020) were associated with raised coronary calcium score.
Patients with NLRP12 germline mutations and diagnosis of NLRP12-related autoinflammatory disease demonstrated highly variable clinical phenotypes.
report the crystal structure of NLRP12 PYD domain at 1.70 A fused with an maltose-binding protein (MBP) tag
all of the reported mutations were found to have occurred in a highly conserved region in the NACHT domain coding sequence in NLRP12 exon 3, suggesting that a screening strategy for Familial cold autoinflammatory syndrome should focus on this area of the gene
The novel findings reveal the critical role of NLRP12-IL-17A-CXCL1 axis in host defense by modulating neutrophil recruitment against Klebsiella pneumoniae.
This process involved the upregulation of NLRP12.
NLRX1, NLRP12 and NLRC3 negatively modulate the host immune response following virus exposure. (Review)
Variants of NLRP12 were associated with common variable immunodeficiency.
NLRP12/NLRP3-dependent activation of caspase-1 is likely to be a key event in mediating systemic production of IL-1beta and hypersensitivity to secondary bacterial infection during malaria.
The genetics, expression and roles of NLRP12 in inflammatory signaling, host defense, and carcinogenesis are reviewed. Review.
This study suggested that NLRP12 mutations might account for a small fraction of common variable immunodeficiency patients with severe auto-inflammatory complications.
We will focus on NLRP6 and NLRP12.
Letter: NLRP12 mutations associated with familial cold autoinflammatory syndrome 2 in Italian patients.
Even with a variable range of associated manifestations, the extreme sensitivity to cold represents the main clinical hallmark in an individual carrying the p.D294E mutation of the NLRP12 gene.
The authors report the first in vitro confirmed non-homotypic interaction between NLRP12 pyrin domain and the pro-apoptotic protein Fas-associated factor 1 (FAF-1), which links the innate immune system to apoptotic signaling.
NLRP12 missense mutation in periodic fever syndromes; study provides evidence of deleterious effect of an NLRP12 missense mutation; this newly identified molecular defect emphasizes the crucial role played by NLRP12 in autoinflammation
regulates activation of NF-kappa B and caspase-1-dependent cytokine processing
Monarch-1 enhances nonclassical and classical major histocompatibility complex class I expression at the level of the promoter, RNA, and protein expression.
Monarch-1 associates with IRAK-1 but not MyD88, resulting in the blockage of IRAK-1 hyperphosphorylation
NLRP12 enhances noncanonical NF-kappaB signaling through inhibition of ERK1/2 signaling, thereby promoting neutrophil differentiation.
Nlrp12(-/-) mice show increased weight gain, adipose deposition, blood glucose, NF-kappaB/MAPK activation, and M1-macrophage polarization.
NLRP12 promotes bacterial tolerance via degradation of NOD2 through the Ubiquitin-Proteasome Pathway
the data demonstrate a previously unappreciated role for Nlrp12 in exacerbating the pathogenesis of influenza A virus infection through the regulation of CXCL1-mediated neutrophilic responses.
The results demonstrate that C57BL/6J mice have a functional defect in NLRP12, impaired CXCL1 production, and that macrophages require NLRP12 expression for effective recruitment of neutrophils to inflammatory sites.
Data show that TLR4-mediated up-regulation of Blimp-1 led to the down-regulation of NLRP12 expression in dextran sulfate sodium (DSS)-induced colitis.
this study shows that NLRP12 is essential for survival after radiation and thermal combined injury by regulating myelopoiesis and immune reconstitution
our findings suggest that NLRP12 plays an important role in negatively regulating the early inflammatory responses against B. abortus.
this study reveals a feed-forward loop in which NLRP12 promotes specific commensals that can reverse gut inflammation, while cytokine blockade during NLRP12 deficiency can reverse dysbiosis
Ambient fine particulate matter-induced myocarditis is mediated by EGFR/Akt signaling and overexpression of NLRP3 and NLRP12.
Nlrp12 deficiency caused increased neutrophil migration towards the chemokine CXCL1 and the neutrophil parasite Leishmania major, revealing NLRP12 as a negative regulator of directed neutrophil migration under these conditions.
modulation of NLRP12 levels controls alternative NF-kappaB signaling in OC precursors, altering bone homeostasis and osteolytic responses
The absence of Nlrp12 results in an increased inflammatory response
NLRP12 is an intrinsic negative regulator of T-cell-mediated immunity via altered NF-kappaB regulation and IL-4 production as key mediators of NLRP12-associated disease.
The role of NLRP12 in NF-KB signaling, bacterial infections, colitis, colorectal tumorigenesis and gut homeostasis is studied in knockout mice. Review.
NLRP12-deficient mice are highly resistant to S. typhimurium infection, which highlights the signaling pathway defined by NLRP12-mediated dampening of host immune defenses that could be exploited by S. typhimurium to persist and survive in the host
NLRP12 does not significantly contribute to the in vivo host innate immune response to LPS stimulation, Klebsiella pneumonia infection or Mycobacterium tuberculosis
NLRP12 negatively regulated ERK and AKT signaling pathways in affected tumor tissues.
This gene encodes a member of the CATERPILLER family of cytoplasmic proteins. The encoded protein, which contains an N-terminal pyrin domain, a NACHT domain, a NACHT-associated domain, and a C-terminus leucine-rich repeat region, functions as an attenuating factor of inflammation by suppressing inflammatory responses in activated monocytes. Mutations in this gene cause familial cold autoinflammatory syndrome type 2. Alternative splicing results in multiple transcript variants.
NACHT, leucine rich repeat and PYD containing 12
, NLR family, pyrin domain containing 12
, PYRIN-containing APAF1-like protein 7
, NACHT, LRR and PYD domains-containing protein 12
, NLR family, pyrin domain containing 12, isoform 2
, monarch 1
, nucleotide-binding oligomerization domain, leucine rich repeat and pyrin domain containing 12
, regulated by nitric oxide
, NACHT, LRR and PYD containing protein 12