NALP1 Antibody (YA8914)
(Synonyms: CARD7, DEFCAP, KIAA0926, NAC, NALP1, NLRP1, Caspase recruitment domain-containing protein 7, Death effector filament-forming ced-4-like apoptosis protein, Nucleotide-binding domain and caspase recruitment domain)Based on 1 Customer Validation
NALP1 Antibody (YA8914) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to NALP1.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, ICC/IF, IF-Tissue, IP, ELISA
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Reactivity :
human, mouse, rat
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Formulation:
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% 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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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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IP
IP: Immunoprecipitation
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|---|
| Dilution Ratio | 1:100-1000 | 1:50-500 | 1:50-500 | 1-2μg per 100-500μg Total protein | 1:30-3000 |
Product Details
NALP1 Antibody (YA8914) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to NALP1.
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Host Mouse
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Species Reactivityhuman, mouse, rat
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Calculated Molecular Weight Predicted band size: 162 kDa
OMIM: 606636
A synthesized peptide derived from human NALP1.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at 2-8°C for 1 year, do not freeze.
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Shipping
Shipping with blue ice.
Verification Images
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Western blot analysis was performed on protein extracts (25 μg) from SH-SY5Y (lane 1), Ramos (lane 2) and MCF-7 (lane 3) using NALP1 antibody. Proteins were transferred onto a 0.45 μm PVDF membrane using the Trans-Blot® Turbo™ system for 13 min. The membrane was then blocked with 5% nonfat milk in TBST (HY-K1025) for 1 h at room temperature. The primary antibody (1:1000) and loading control antibody GAPDH Antibody (HRP) (HY-P80954A) (1:5000) were diluted in 5% nonfat milk in TBST and incubated with the membrane overnight at 4°C. After washing, the membrane of primary antibody was incubated with HRP-conjugated goat anti-rabbit/mouse IgG secondary antibody (HY-P8001/HY-P8004) (1:5000) diluted in 5% nonfat milk in TBST for 1 h at room temperature. Protein bands were visualized using an Ultra High Sensitivity ECL detection kit (HY-K1005).
Background
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Function
NALP1 acts as the sensor component of the NLRP1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. 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. Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as cleavage by some human enteroviruses and rhinoviruses, double-stranded RNA, UV-B irradiation, or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex composed of NLRP1, CASP1 and PYCARD/ASC. In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and associates with PYCARD/ASC to initiate the formation of the inflammasome complex: the NLRP1 inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis. In the absence of GSDMD expression, the NLRP1 inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME). Activation of NLRP1 inflammasome is also required for HMGB1 secretion; the active cytokines and HMGB1 stimulate inflammatory responses. Binds ATP and shows ATPase activity. Plays an important role in antiviral immunity and inflammation in the human airway epithelium. Specifically recognizes a number of pathogen-associated signals: upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion. Positive-strand RNA viruses, such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion. Acts as a direct sensor for long dsRNA and thus RNA virus infection. May also be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner. The NLRP1 inflammasome is also activated in response to UV-B irradiation causing ribosome collisions: ribosome collisions cause phosphorylation and activation of NLRP1 in a MAP3K20-dependent manner, leading to pyroptosis[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21].
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Subcellular Localization
Cytoplasm, cytosol; Cytoplasm; Nucleus
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Expression
Tissue_Specificity: Widely expressed. Abundantly expressed in primary immune cells (isoform 1 and isoform 2), including in neutrophils, monocytes/macrophages, dendritic cells (mostly Langerhans cells), and B- and T-lymphocytes (at protein level). Strongly expressed in epithelial cells lining the glandular epithelium, such as that of the gastrointestinal tract (stomach, small intestine, colon), the respiratory tract (trachea and bronchi), and the endometrial and endocervical glands, gallbladder, prostate, and breast (at protein level). In testis, expressed in spermatogonia and primary spermatocytes, but not in Sertoli cells (at protein level). In the brain, expressed in neurons, in particular in pyramidal ones and in oligodendrocytes, but not detected in microglia (at protein level). Expressed in adult and fetal ocular tissues, including in adult and 24-week old fetal choroid, sclera, cornea, and optic nerve, as well as in adult retina and fetal retina/retinal pigment epithelium. Highly expressed in the skin throughout the epidermis and in dermal fibroblasts, in both glabrous skin and plantar skin. It is detected in keratinocytes, but not in melanocytes. Expressed in epidermal appendages such as hair follicles.
Induction: Up-regulated by ATF4 during endoplasmic reticulum (ER) stress response. Up-regulated in arterial endothelial cells exposed to plasma from patients with peripheral arterial disease, but not to plasma from healthy controls. -
Isoforms & Post-Translational Modification
NALP1 has 5 isoforms, Q9C000-1: amino acid length is 1473, molecular weight is 165866 Da (predicted); Q9C000-2: amino acid length is 1429, molecular weight is 160946 Da (predicted); Q9C000-3: amino acid length is 1399, molecular weight is 157319 Da (predicted); Q9C000-4: amino acid length is 1443, molecular weight is 162239 Da (predicted); Q9C000-5: amino acid length is 1375, molecular weight is 154881 Da (predicted).
Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. -
Subunit
Interacts (via LRR repeats) with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3); these interactions reduce NLRP1 inflammasome-induced CASP1 activation and IL1B release, possibly by impairing NLRP1 interaction with PYCARD.
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SwissProt ID
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Synonyms
CARD7, DEFCAP, KIAA0926, NAC, NALP1, NLRP1, Caspase recruitment domain-containing protein 7, Death effector filament-forming ced-4-like apoptosis protein, Nucleotide-binding domain and caspase recruitment domain
Documentation
References
[1]. Martinon F, et al. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 2002 Aug;10(2):417-26. [Content Brief]
[2]. Faustin B, et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell. 2007 Mar 9;25(5):713-24. [Content Brief]
[3]. Finger JN, et al. Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity. J Biol Chem. 2012 Jul 20;287(30):25030-7. [Content Brief]
[4]. Zhong FL, et al. Germline NLRP1 Mutations Cause Skin Inflammatory and Cancer Susceptibility Syndromes via Inflammasome Activation. Cell. 2016 Sep 22;167(1):187-202.e17. [Content Brief]
[5]. Drutman SB, et al. Homozygous NLRP1 gain-of-function mutation in siblings with a syndromic form of recurrent respiratory papillomatosis. Proc Natl Acad Sci U S A. 2019 Sep 17;116(38):19055-19063. [Content Brief]
[6]. Robinson KS, et al. Enteroviral 3C protease activates the human NLRP1 inflammasome in airway epithelia. Science. 2020 Dec 4;370(6521):. [Content Brief]
[7]. Tsu BV, et al. Diverse viral proteases activate the NLRP1 inflammasome. Elife. 2021 Jan 7;10:. [Content Brief]
[8]. Huang M, et al. Structural and biochemical mechanisms of NLRP1 inhibition by DPP9. Nature. 2021 Apr;592(7856):773-777. [Content Brief]
[9]. Hollingsworth LR, et al. DPP9 sequesters the C terminus of NLRP1 to repress inflammasome activation. Nature. 2021 Apr;592(7856):778-783. [Content Brief]
[10]. Robinson KS, et al. ZAKα-driven ribotoxic stress response activates the human NLRP1 inflammasome. Science. 2022 Jul 15;377(6603):328-335. [Content Brief]
[11]. Sollberger G, et al. Caspase-1 activity is required for UVB-induced apoptosis of human keratinocytes. J Invest Dermatol. 2015 May;135(5):1395-1404. [Content Brief]
[12]. Fenini G, et al. Genome Editing of Human Primary Keratinocytes by CRISPR/Cas9 Reveals an Essential Role of the NLRP1 Inflammasome in UVB Sensing. J Invest Dermatol. 2018 Dec;138(12):2644-2652. [Content Brief]
[13]. Zhong FL, et al. Human DPP9 represses NLRP1 inflammasome and protects against autoinflammatory diseases via both peptidase activity and FIIND domain binding. J Biol Chem. 2018 Dec 7;293(49):18864-18878. [Content Brief]
[14]. Bauernfried S, et al. Human NLRP1 is a sensor for double-stranded RNA. Science. 2021 Jan 29;371(6528):. [Content Brief]
[15]. Ball DP, et al. Caspase-1 interdomain linker cleavage is required for pyroptosis. Life Sci Alliance. 2020 Mar;3(3):. [Content Brief]
[16]. Zhou B, et al. Gasdermin E permits interleukin-1 beta release in distinct sublytic and pyroptotic phases. Cell Rep. 2021 Apr 13;35(2):108998. [Content Brief]
[17]. Planès R, et al. Human NLRP1 is a sensor of pathogenic coronavirus 3CL proteases in lung epithelial cells. Mol Cell. 2022 Jul 7;82(13):2385-2400.e9. [Content Brief]
[18]. Lu B, et al. Novel role of PKR in inflammasome activation and HMGB1 release. Nature. 2012 Aug 30;488(7413):670-4. [Content Brief]
[19]. Chu ZL, et al. A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis. J Biol Chem. 2001 Mar 23;276(12):9239-45. [Content Brief]
[20]. Liu F, et al. Expression of NALP1 in cerebellar granule neurons stimulates apoptosis. Cell Signal. 2004 Sep;16(9):1013-21. [Content Brief]
[21]. Hsu LC, et al. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide. Proc Natl Acad Sci U S A. 2008 Jun 3;105(22):7803-8. [Content Brief]
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