TNKS monoclonal antibody, clone 19A449
- Known as:
- TNKS mab (anti-), clonality 19A449
- Catalog number:
- MAB8037
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- TNKS monoclonal antibody clone 19A449
Related genes to: TNKS monoclonal antibody, clone 19A449
- Gene:
- TNKS NIH gene
- Name:
- tankyrase
- Previous symbol:
- -
- Synonyms:
- TIN1, TINF1, TNKS1, PARP-5a, PARP5A, pART5
- Chromosome:
- 8p23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-08
- Date modifiied:
- 2016-03-01
Related products to: TNKS monoclonal antibody, clone 19A449
Related articles to: TNKS monoclonal antibody, clone 19A449
- Although tankyrases (TNKSs) were originally described as enzymes safeguarding genome integrity, TNKSs are also associated with metabolism and are involved in the differentiation of multiple cell lineages including adipocytes. Here we aimed to understand the role of TNKSs specifically in adipocyte differentiation. We found that the deletion of TNKS1 or TNKS2 decreased the rate of adipocyte differentiation. Furthermore, the loss of TNKs induced a multi-pronged cellular adaptation characterized by changes in cellular proteostasis centered around the inhibition of autophagy, AMPK activation and the suppression of mTORC1 activity. Deleting TNKSs also induced mitochondrial oxidative phosphorylation and glycolytic flux. Interestingly, the fraction of oligomycin-resistant respiration decreased, suggesting more coupled OXPHOS. However, the lower differentiation rate of TNKS2 knockout cells was salvaged by pharmacological activation of autophagy (by NV-5138) and the pharmacological inhibition of LKB1 (by HY-10371), an upstream suppressor of the mTOR system. Finally, TNKS2 can ADP-ribosylate LKB1, rendering it susceptible for ubiquitinylation that appears to be a key step towards committing adipocytes to differentiation. Together this data validates the use of TNK inhibitors for managing metabolic diseases and raises the possibility that TNK inhibition can influence tumor or immunometabolism and amplify the effects of other treatments. - Source: PubMed
Publication date: 2026/08/06
Rauch BoglarkaUjlaki GyulaPoliska SzilardMurahwa NakayiKovacs PatrikPettko-Szandtner AladarUray KarenBai Peter - Poly(ADP-ribose) or PAR regulates multiple aspects of cell biology, both as an independent signaling molecule and as a modification on biomolecules. As a posttranslational modification, PAR can modulate the biochemical properties of target proteins. Isolated free PAR molecules function in cellular signaling. This chapter describes two methods to isolate and purify free PAR and protein-linked PAR from biochemical reactions, one using chemical fractionation and another using physical separation. A method to isolate free PAR and protein-linked PAR from human cells is also presented. These methods allow monitoring of free PAR and protein-linked PAR levels under different biochemical conditions or in response to different cellular stimuli. - Source: PubMed
Langelier Marie-FranceMirhasan ManijaPascal John M - Tankyrases (TNKS1/2) are multi-domain poly(ADP-ribose) polymerases that regulate Wnt/β-catenin signaling and broader cellular programs through both catalytic activity and extensive protein-protein interaction (PPI) networks. While most tankyrase-directed drug discovery has focused on inhibiting the PARP catalytic site, an emerging alternative is to target tankyrase stability by disrupting its interaction with the deubiquitinase USP25. USP25 functions as a positive regulator of tankyrase abundance by counteracting ubiquitin-dependent turnover; consequently, blocking the TNKS-USP25 PPI can reduce tankyrase levels, stabilize pathway antagonists such as AXIN, and dampen Wnt transcriptional output. In this review, we discuss current understanding of tankyrase domain architecture with emphasis on ankyrin repeat clusters (ARC1/2/4/5) that recognize short tankyrase-binding motifs (TBMs), and we highlight why ARC5 is a particularly actionable node for intervention in the TNKS-USP25 axis. We summarize the structural basis of USP25 recruitment a C-terminal TBM-like element, discuss ARC hotspot features that support ligandability, and provide a practical chemical-biology framework for validating PPI disruption using orthogonal assays (co-immunoprecipitation/proximity ligation, biophysics such as SPR/ITC, cellular target engagement, and displacement formats including FP/FRET). We then evaluate reported small-molecule disruptors, including C44 and UAT-B, as proof-of-concept agents that link ARC5-centered binding to tankyrase destabilization and antitumor phenotypes in prostate cancer and multidrug-resistant colorectal cancer models. Finally, we outline key challenges-selectivity across ARCs, off-target risk, and context-dependent biology-and propose future directions, including structure-guided optimization, improved cell-active chemotypes, and dual-mechanism strategies that combine PPI disruption with catalytic inhibition or targeted degradation approaches. - Source: PubMed
Publication date: 2026/07/06
Kamel Emadeldin MKhadrawy Sally MostafaAli Mohamed A MAhmed Noha AAlkhedhairi SalehAba Alkhayl Faris FLamsabhi Al Mokhtar - Chemotherapy remains the most preferred therapeutic option for Triple-Negative breast cancer (TNBC), but patients frequently develop resistance over time, which remains a major clinical challenge, leading to poor patient treatment outcomes. - Source: PubMed
Publication date: 2026/07/09
Jan ShariqaFatima KaneezKhan Sameer UllahMalik Fayaz A - Amyotrophic Lateral Sclerosis (ALS) is a rare and fatal neurodegenerative disease characterized by the hallmark cytoplasmic accumulation and aggregation of TAR DNA binding protein 43 (TDP-43), which impairs proteasome activity through its interaction with Tankyrase (TNKS). Using molecular and imaging techniques, we have identified a novel role for the Fragile X Mental Retardation Protein (FMRP) in regulating the TNKS/PI31-mediated proteasome activation mechanism in co-operation with TDP-43. Our results demonstrate that depletion of FMRP causes nuclear translocation of TDP-43, reducing cytoplasmic TNKS/TDP-43 co-localization, thereby releasing TNKS in the cytoplasm. Free TNKS gets associated with proteasome inhibitor of 31 kDa (PI31), reversing PI31-mediated inhibition of proteasome assembly, trafficking, and activity. Thus, FMRP regulates proteasome activity by modulating the subcellular distribution of TDP-43. Interestingly, FMRP expression is elevated in specific brain regions and spinal cords of TDP-43 transgenic ALS mice that helps more TDP-43 to stay in cytoplasm to sequester more TNKS with it, resulting in proteasome dysfunction in ALS disease system. We have demonstrated for the first time that FMRP can act as a disease modifier for ALS. ALS patients with high FMRP expression in the brain and spinal cord may exhibit more severe protein aggregation due to proteasome dysfunction. - Source: PubMed
Majumder PrithaAhsan AsmarBubphachat PitchapaAkter KhadizaHuang Jeffrey KHuang Chi-Chen Sarah