Product: TMS1/ASC Antibody
Catalog: DF6304
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse, Rat
Prediction: Bovine, Horse, Sheep, Rabbit
Mol.Wt.: 15~25kD; 22kD(Calculated).
Uniprot: Q9ULZ3
RRID: AB_2838270

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Bovine(100%), Horse(90%), Sheep(100%), Rabbit(90%)
PYCARD Antibody detects endogenous levels of total TMS1/ASC.
Cite Format: Affinity Biosciences Cat# DF6304, RRID:AB_2838270.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


Apoptosis associated speck like protein containing a CARD; Apoptosis-associated speck-like protein containing a CARD; ASC; ASC_HUMAN; CARD 5; CARD5; Caspase recruitment domain containing protein 5; Caspase recruitment domain protein 5; Caspase recruitment domain-containing protein 5; hASC; MGC10332; PYCARD; PYD and CARD domain containing; PYD and CARD domain containing protein; PYD and CARD domain-containing protein; Target of methylation induced silencing 1; Target of methylation-induced silencing 1; TMS 1; TMS; TMS1;



Widely expressed at low levels. Detected in peripheral blood leukocytes, lung, small intestine, spleen, thymus, colon and at lower levels in placenta, liver and kidney. Very low expression in skeletal muscle, heart and brain. Expressed in lung epithelial cells (at protein level) (PubMed:23229815). Detected in the leukemia cell lines HL-60 and U-937, but not in Jurkat T-cell lymphoma and Daudi Burkitt's lymphoma. Detected in the melanoma cell line WM35, but not in WM793. Not detected in HeLa cervical carcinoma cells and MOLT-4 lymphocytic leukemia cells.

TMS1 (target of methylation-induced silencing)/ASC (apoptosis-associated speck-like protein containing a CARD), also referred to as PYCARD and CARD5, is a 22-kDa pro-apoptotic protein containing an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD) (1-2). The TMS1 gene was originally found to be aberrantly methylated and silenced in breast cancer cells (2), and has since been found to be silenced in a number of other cancers, including ovarian cancer (3), glioblastoma (4), melanoma (5), gastric cancer (6), lung cancer (7), and prostate cancer (8). Expression of TMS1 can be induced by pro-apoptotic/inflammatory stimuli (9). During apoptosis TMS1 is re-distributed from the cytosol to the mitochondria and associates with mitochondrial Bax to trigger cytochrome c release and subsequent apoptosis (10). TMS1 has also been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (11).



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q9ULZ3 As Substrate

Site PTM Type Enzyme
K21 Acetylation
K21 Ubiquitination
K22 Ubiquitination
S46 Phosphorylation
S58 Phosphorylation
K109 Ubiquitination
K139 Ubiquitination
Y146 Phosphorylation P43405 (SYK) , Q14289 (PTK2B)
S164 Phosphorylation
Y187 Phosphorylation P43405 (SYK)
S195 Phosphorylation

Research Backgrounds


Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. Isoform 2 may have a regulating effect on the function as inflammasome adapter. Isoform 3 seems to inhibit inflammasome-mediated maturation of interleukin-1 beta. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.



Subcellular Location:

Cytoplasm. Endoplasmic reticulum. Mitochondrion. Nucleus.
Note: Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection. Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis (By similarity).

Golgi apparatus membrane.
Note: (Microbial infection) Upon HRSV infection, the protein is mainly located in lipid rafts in the Golgi membrane.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Widely expressed at low levels. Detected in peripheral blood leukocytes, lung, small intestine, spleen, thymus, colon and at lower levels in placenta, liver and kidney. Very low expression in skeletal muscle, heart and brain. Expressed in lung epithelial cells (at protein level). Detected in the leukemia cell lines HL-60 and U-937, but not in Jurkat T-cell lymphoma and Daudi Burkitt's lymphoma. Detected in the melanoma cell line WM35, but not in WM793. Not detected in HeLa cervical carcinoma cells and MOLT-4 lymphocytic leukemia cells.

Subunit Structure:

Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta secretion. Homooligomers can form disk-like particles of approximately 12 nm diameter and approximately 1 nm height. Next to isoform 1, also isoform 2 and isoform 3 may be involved in oligomerization leading to functional regulation. Component of several inflammasomes containing one pattern recognition receptor/sensor, such as NLRP1, NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or IFI16. Major component of the ASC pyroptosome, a 1-2 um supramolecular assembly (one per macrophage cell) which consists of oligomerized PYCARD dimers and CASP1. Interacts with CASP1 (precursor form); the interaction induces activation of CASP1 leading to the processing of interleukin-1 beta; PYCARD competes with RIPK2 for binding to CASP1. Interacts with NLRP3; the interaction requires the homooligomerization of NLRP3. Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2, PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX.


The CARD domain mediates interaction with CASP1 and NLRC4 (PubMed:14634131 and PubMed:11967258).

The pyrin domain mediates homotypic interactions with pyrin domains of proteins such as of NLRP3, PYDC1, PYDC2 and AIM2.

Research Fields

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Salmonella infection.

· Human Diseases > Infectious diseases: Bacterial > Pertussis.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Viral > Influenza A.

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Cytosolic DNA-sensing pathway.   (View pathway)


1). Wu K et al. The gut microbial metabolite trimethylamine N-oxide aggravates GVHD by inducing M1 macrophage polarization in mice. Blood 2020 Jul 23;136(4):501-515. (PubMed: 32291445) [IF=25.476]

Application: IF/ICC    Species: mouse    Sample: BMDMs

Figure 5.| TMAO enhanced M1 polarization via activating NLRP3 inflammasome. (A) Representative immunofluorescence staining of NLRP3 (green: Alexa Fluor 488), ASC (red: Alexa Fluor 594), DAPI (blue) on BMDMs after TMAO (300M) stimulation for 24hrs. Scale bar=5μm.

2). Wang Y et al. Overexpression of NAG-1/GDF15 prevents hepatic steatosis through inhibiting oxidative stress-mediated dsDNA release and AIM2 inflammasome activation. Redox Biol 2022 Jun;52:102322. (PubMed: 35504134) [IF=10.787]

3). Hong Z et al. The ROS/GRK2/HIF-1α/NLRP3 Pathway Mediates Pyroptosis of Fibroblast-Like Synoviocytes and the Regulation of Monomer Derivatives of Paeoniflorin. Oxid Med Cell Longev 2022 Jan 29;2022:4566851. (PubMed: 35132350) [IF=7.310]

4). Lin JQ et al. Zinc provides neuroprotection by regulating NLRP3 inflammasome through autophagy and ubiquitination in a spinal contusion injury model. CNS Neurosci Ther 2020 Oct 9. (PubMed: 33034415) [IF=7.035]

Application: WB    Species: mouse    Sample:

FIGURE 4 |Treatment with zinc suppresses the NLRP3 inflammasome after SCI Mice were sacrificed on the third day after zinc administration.(A)Representative Western blot analysis of NLRP3 inflammasome in Sham, SCI + vehicle and SCI + zinc group(n = 6).

5). Lin X et al. Ameliorate effect of pyrroloquinoline quinone against cyclophosphamide-induced nephrotoxicity by activating the Nrf2 pathway and inhibiting the NLRP3 pathway. Life Sci 2020 Jun 3;256:117901. (PubMed: 32504759) [IF=6.780]

Application: WB    Species: mouse    Sample: kidney

Fig. 7. |Effect of PQQ on protein expression in the NLRP3 inflammatory pathway. The expression levels of NLRP3 (A), ASC (B), and Caspase-1 (C). Data are shown as mean ± SD, n = 8. #p < 0.05 and ##p < 0.01 versus the Control group. ⁎p < 0.05 and ⁎⁎p < 0.01 versus the Model group.

6). Guan L et al. Puerarin ameliorates retinal ganglion cell damage induced by retinal ischemia/reperfusion through inhibiting the activation of TLR4/NLRP3 inflammasome. Life Sci 2020 Jun 8;117935. (PubMed: 32526286) [IF=6.780]

7). Zhou J et al. EB1089 promotes the expression of vitamin D receptor in the intestinal epithelial cell line HT-29 and reduces lipopolysaccharide-induced inflammatory response. Mol Med 2022 Jan 3;28(1):1. (PubMed: 34979900) [IF=6.376]

8). Chen J et al. Sonneratia apetala seed oil attenuates potassium oxonate/hypoxanthine-induced hyperuricemia and renal injury in mice. Food Funct 2021 Oct 4;12(19):9416-9431. (PubMed: 34606558) [IF=6.317]

9). Wang X et al. Microglial NLRP3 inflammasome activation promotes prolactinomas development. Endocr Relat Cancer 2021 May 1;ERC-21-0137. (PubMed: 33974557) [IF=5.900]

10). Ma B et al. Yanghe Decoction Suppresses the Experimental Autoimmune Thyroiditis in Rats by Improving NLRP3 Inflammasome and Immune Dysregulation. Front Pharmacol 2021 Jun 21;12:645354. (PubMed: 34234669) [IF=5.810]

Application: WB    Species: Rat    Sample: peripheral blood mononuclear cell (PBMCs)

FIGURE 8 Western blot analysis of NLRP3 inflammasome cascade in thyroid (A) Western blotting images of IL-17, p-NF-κB, NF-κB, NLRP3, ASC, cleaved-Caspase1, pro-Caspase 1, pro-IL-1β, cleaved-IL-1β, and IL-18: Lane 1, control group; lane 2, model group; lane 3, YH 5 g crude drug/kG group; lane 4, YH 15 g crude drug/kG group; lane 5, selenious group. Bar graphs indicate the relative ratio of IL-17 over tubulin (B), p-NF-κB over NF-κB (C), NLRP3 over tubulin (D), ASC over tubulin (E), cleaved-Caspase-1 over pro-Caspase-1 (F), cleaved-IL-1β over pro-IL-1β (G), and IL-18 over tubulin (H) in thyroid. All values are expressed as mean ± SEM. *p < 0.05, **p < 0.01 vs Model.

Load more

Restrictive clause


Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.