NLRP3 Antibody (YA9972)
(Synonyms: C1orf7, CIAS1, NALP3, PYPAF1, NLRP3, Angiotensin/vasopressin receptor AII/AVP-like, Caterpiller protein 1.1, Cold-induced autoinflammatory syndrome 1 protein, Cryopyrin, PYRIN-containing APAF1-like protein 1, CLR1.1)NLRP3 Antibody (YA9972) is a Rabbit-derived and non-conjugated IgG Monoclonal antibody, targeting to NLRP3 Antibody.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, containing 50% glycerol, 0.2% BSA and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 | 1:100-200 |
Product Details
NLRP3 Antibody (YA9972) is a Rabbit-derived and non-conjugated IgG Monoclonal antibody, targeting to NLRP3 Antibody.
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Host Rabbit
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Clonality Monoclonal,Recombinant
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 118 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 118 kDa
Entrez Gene: 114548 Human ; 216799 Mouse ; 287362 Rat
SwissProt: Q96P20 Human ; Q8R4B8 Mouse ; D4A523 Rat
OMIM: 120100 Human
Synthetic peptide corresponding to human NLRP3.
Endogenous
affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, containing 50% glycerol, 0.2% BSA and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
NLRP3 is a Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis. In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC. Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis. Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses. Involved in the homeostatic wound healing response to tissue injury, a multistep cascade that guides neutrophil migration to necrotic sites while avoiding collateral damage of healthy tissues. ATP released from necrotic cells triggers activation of NLRP3 inflammasome through P2RX7 signaling leading to neutrophil adhesion to the vascular endothelium close to the injury site (By similarity). Under resting conditions, ADP-bound NLRP3 is autoinhibited. NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc. Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex. Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P). Shows ATPase activity[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29].
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Subcellular Localization
Cytoplasm, cytosol; Inflammasome; Cytoplasm, cytoskeleton, microtubule organizing center; Golgi apparatus membrane; Endoplasmic reticulum; Mitochondrion; Secreted; Nucleus
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Expression
Tissue_Specificity: Predominantly expressed in macrophages. Also expressed in dendritic cells, B- and T-cells (at protein level). Expressed in LPS-treated granulocytes, but not in resting cells (at protein level). Expression in monocytes is very weak (at protein level). Expressed in stratified non-keratinizing squamous epithelium, including oral, esophageal and ectocervical mucosa and in the Hassall's corpuscles in the thymus. Also, detected in the stratified epithelium covering the bladder and ureter (transitional mucosa) (at protein level). Expressed in lung epithelial cells (at protein level). Expressed in chondrocytes. Expressed at low levels in resting osteoblasts.
Induction: By activators of Toll-like receptors, such as lipoteichoic acid (LTA) (TLR2), polyinosine-polycytidylic acid (poly(I:C), a synthetic analog of dsRNA) (TLR3) and bacterial lipopolysaccharides (LPS) (TLR4), and by TNF. Up-regulated in osteoblasts after exposure to invasive, but not invasion-defective, strains of Salmonella typhimurium (at protein level). In macrophages, up-regulated by endocannabinoid anandamide/AEA. -
Isoforms & Post-Translational Modification
NLRP3 has 6 isoforms, Q96P20-1: amino acid length is 1036, molecular weight is 118173 Da (predicted); Q96P20-2: amino acid length is 922, molecular weight is 105975 Da (predicted); Q96P20-3: amino acid length is 719, molecular weight is 83533 Da (predicted); Q96P20-4: amino acid length is 979, molecular weight is 111884 Da (predicted); Q96P20-5: amino acid length is 979, molecular weight is 112263 Da (predicted); Q96P20-6: amino acid length is 1016, molecular weight is 115968 Da (predicted).
Phosphorylation at Ser-198 by MAPK8/JNK1 increases inflammasome activation by promoting deubiquitination by BRCC3 and NLRP3 homooligomerization. Phosphorylation at Ser-806 by CSNK1A1 prevents inflammasome activation by preventing NEK7 recruitment. Phosphorylation by ERK1/MAPK3 promotes NLRP3 inflammasome assembly. Phosphorylation by BTK (at Tyr-136, Tyr-140, Tyr-143 and Tyr-168) in the region that mediates binding to phosphatidylinositol phosphate, promotes relocalization of NLRP3 and assembly of the NLRP3 inflammasome. Phosphorylation at Tyr-861 inhibits NLRP3 inflammasome assembly: dephosphorylation by PTPN22 promotes inflammasome activation. Phosphorylated by LATS1 and LATS2 at Ser-265 following palmitoylation by ZDHHC1, promoting its relocalization to the microtubule organizing center (MTOC), where NLRP3 is activated by NEK7, leading to inflammasome assembly and activation. -
Subunit
Sensor component of NLRP3 inflammasomes; inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation.
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SwissProt ID
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Synonyms
C1orf7, CIAS1, NALP3, PYPAF1, NLRP3, Angiotensin/vasopressin receptor AII/AVP-like, Caterpiller protein 1.1, Cold-induced autoinflammatory syndrome 1 protein, Cryopyrin, PYRIN-containing APAF1-like protein 1, CLR1.1
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Research Field
Immunology
Documentation
References
[1]. Martinon F, et al. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature. 2006 Mar 9;440(7081):237-41. [Content Brief]
[2]. Dostert C, et al. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science. 2008 May 2;320(5876):674-7. [Content Brief]
[3]. Hornung V, et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 2008 Aug;9(8):847-56. [Content Brief]
[4]. Subramanian N, et al. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 2013 Apr 11;153(2):348-61. [Content Brief]
[5]. Coll RC, et al. A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases. Nat Med. 2015 Mar;21(3):248-55. [Content Brief]
[6]. Song H, et al. The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3. Nat Commun. 2016 Dec 8;7:13727. [Content Brief]
[7]. Li X, et al. MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism. Nat Commun. 2017 Jun 28;8:15986. [Content Brief]
[8]. Nakanishi H, et al. NLRP3 mutation and cochlear autoinflammation cause syndromic and nonsyndromic hearing loss DFNA34 responsive to anakinra therapy. Proc Natl Acad Sci U S A. 2017 Sep 12;114(37):E7766-E7775. [Content Brief]
[9]. Chen J, et al. PtdIns4P on dispersed trans-Golgi network mediates NLRP3 inflammasome activation. Nature. 2018 Dec;564(7734):71-76. [Content Brief]
[10]. Mehto S, et al. The Crohn's Disease Risk Factor IRGM Limits NLRP3 Inflammasome Activation by Impeding Its Assembly and by Mediating Its Selective Autophagy. Mol Cell. 2019 Feb 7;73(3):429-445.e7. [Content Brief]
[11]. Coll RC, et al. MCC950 directly targets the NLRP3 ATP-hydrolysis motif for inflammasome inhibition. Nat Chem Biol. 2019 Jun;15(6):556-559. [Content Brief]
[12]. Tapia-Abellán A, et al. MCC950 closes the active conformation of NLRP3 to an inactive state. Nat Chem Biol. 2019 Jun;15(6):560-564. [Content Brief]
[13]. Sharif H, et al. Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome. Nature. 2019 Jun;570(7761):338-343. [Content Brief]
[14]. Rodrigues TS, et al. Inflammasomes are activated in response to SARS-CoV-2 infection and are associated with COVID-19 severity in patients. J Exp Med. 2021 Mar 1;218(3):. [Content Brief]
[15]. Theobald SJ, et al. Long-lived macrophage reprogramming drives spike protein-mediated inflammasome activation in COVID-19. EMBO Mol Med. 2021 Aug 9;13(8):e14150. [Content Brief]
[16]. Pan P, et al. SARS-CoV-2 N protein promotes NLRP3 inflammasome activation to induce hyperinflammation. Nat Commun. 2021 Aug 2;12(1):4664. [Content Brief]
[17]. Tang T, et al. The E3 Ubiquitin Ligase TRIM65 Negatively Regulates Inflammasome Activation Through Promoting Ubiquitination of NLRP3. Front Immunol. 2021;12:741839. [Content Brief]
[18]. Xiao L, et al. Cryo-EM structures of the active NLRP3 inflammasome disc. Nature. 2023 Jan;613(7944):595-600. [Content Brief]
[19]. Yang C, et al. Thermal Proteome Profiling Reveals Meltome Upon NLRP3 Inflammasome Activation. Mol Cell Proteomics. 2025 May;24(5):100972. [Content Brief]
[20]. Zhang Y, et al. Human cytomegalovirus protein US18 promotes NLRP3 inflammasome activation. Biochem Biophys Res Commun. 2025 Aug 15;775:152110. [Content Brief]
[21]. Oroz J, et al. ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces. J Biol Chem. 2016 Sep 9;291(37):19487-501. [Content Brief]
[22]. Machtens DA, et al. The Inflammasome Activity of NLRP3 Is Independent of NEK7 in HEK293 Cells Co-Expressing ASC. Int J Mol Sci. 2022 Sep 7;23(18):. [Content Brief]
[23]. Lu B, et al. Novel role of PKR in inflammasome activation and HMGB1 release. Nature. 2012 Aug 30;488(7413):670-4. [Content Brief]
[24]. Hochheiser IV, et al. Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3. Nature. 2022 Apr;604(7904):184-189. [Content Brief]
[25]. Duncan JA, et al. Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome. J Immunol. 2009 May 15;182(10):6460-9. [Content Brief]
[26]. Mitoma H, et al. The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome. Immunity. 2013 Jul 25;39(1):123-35. [Content Brief]
[27]. Nie L, et al. Consecutive palmitoylation and phosphorylation orchestrates NLRP3 membrane trafficking and inflammasome activation. Mol Cell. 2024 Sep 5;84(17):3336-3353.e7. [Content Brief]
[28]. Bittner ZA, et al. BTK operates a phospho-tyrosine switch to regulate NLRP3 inflammasome activity. J Exp Med. 2021 Nov 1;218(11):. [Content Brief]
[29]. Duncan JA, et al. Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling. Proc Natl Acad Sci U S A. 2007 May 8;104(19):8041-6. [Content Brief]
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