Polyclonal Rabbit TP73 Antibody
- Known as:
- Polyclonal Rabbit TP73 Antibody
- Catalog number:
- abx000701
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- Polyclonal Rabbit TP73 Antibody
Related genes to: Polyclonal Rabbit TP73 Antibody
- Gene:
- TP63 NIH gene
- Name:
- tumor protein p63
- Previous symbol:
- TP73L, TP53L, TP53CP
- Synonyms:
- p51, SHFM4, EEC3, p63, p73L, OFC8, KET, p73H, NBP, p53CP
- Chromosome:
- 3q28
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-18
- Date modifiied:
- 2019-04-23
- Gene:
- TP73 NIH gene
- Name:
- tumor protein p73
- Previous symbol:
- -
- Synonyms:
- P73
- Chromosome:
- 1p36.32
- Locus Type:
- gene with protein product
- Date approved:
- 1997-11-12
- Date modifiied:
- 2018-08-08
Related products to: Polyclonal Rabbit TP73 Antibody
Related articles to: Polyclonal Rabbit TP73 Antibody
- Aberrant transcriptional regulation is a defining feature of squamous cell carcinoma (SCC), yet how lineage transcription factors coordinate shared and factor-specific oncogenic programs remains poorly understood. Although TP63 (p63) is frequently amplified in SCC, the contribution of its paralog TP73 (p73) has remained unclear. Here we show that p73, together with p63, is upregulated in skin SCC and is required for tumorigenesis. Mechanistically, p63 and p73 form heteromeric complexes and co-occupy distal enhancer elements, establishing a shared chromatin regulatory framework. Integration of chromatin and transcriptomic profiling reveals that this common enhancer landscape supports both convergent and divergent transcriptional outputs. Both factors cooperatively sustain core proliferation but also exert regulatory biases, with p63 preferentially reinforcing epithelial lineage circuits and p73 contributing to DNA replication and stress-associated pathways. Among shared downstream targets, p63/p73 co-regulation of multiple epidermal growth factor receptor (EGFR) ligands establishes a feed-forward signaling module that amplifies mitogenic signaling. Amphiregulin emerges as a dominant functional mediator, and its depletion phenocopies key aspects of p63/p73 loss, including impaired proliferation and tumor formation. Together, these findings support a model in which shared enhancer occupancy by p63 and p73 drives cooperative and factor-specific transcriptional programs, linking chromatin regulation to signaling and tumor maintenance. - Source: PubMed
Publication date: 2026/02/19
Antonini DarioFerniani MarcoRusso ClaudiaFranciosi MarcoD'Auria LudovicaPalumbo SaraQu JieqiongSouth Andrew PZhou HuiqingKadakia MadhaviDotto Gian PaoloMissero Caterina - Neuroblastoma (NB) is an embryonic malignancy causing 15 % of pediatric cancer fatalities. Amplification of the MYCN gene is one of the major NB drivers and biomarkers of high-risk NB. MYCN amplification is associated with high p53-coding gene expression and decreased survival rates in patients. Importantly, only 1-2 % of NB cases harbor TP53 mutations. Moreover, both high TP53 and low MYC expression levels are unfavorable prognostic markers for NB patients, which is not typical for most types of tumors. In this study we analyzed the effect of MYCN amplification on the expression of genes coding p53 family members - TP63 and TP73. We show that, unlike TP53, TP63 and TP73 levels are higher in MYCN-amplified samples. Furthermore, high TP63 and TP73 expression is a favorable prognostic marker for NB patients' survival. That MDM2 inhibition contributes to p53 stabilization and augments the cytotoxic activity of doxorubicin in NB cells prompted us to test the cytotoxic effects of three small-molecule inhibitors of MDM2 that differ in their mechanisms: Nutlin-3a, Mel23, and SP-141. Our results showed that despite the same target, MDM2, these compounds displayed different cytotoxic effects and synergy with doxorubicin on two widely used NB cell lines, IMR-32 and SH-SY5Y that vary in the amount of MDM2 expression. Collectively, our results suggest that except Nutlin-3a, the other two inhibitors, Mel23 and SP-141, employ additional Mdm2-independent mechanisms of cytotoxicity in NB cells that warrants further investigation. - Source: PubMed
Publication date: 2025/05/10
Nazarov AlexanderParfenyev SergeyShuvalov OlegFrolova KseniaNaminat ElizavetaNevzorov IvanPetukhov AlexeyKarpova NataliaFedorova OlgaBarlev NikolaiDaks Alexandra - Gastric cancer has emerged as one of the major diseases threatening human health. Our previous studies indicated that the anti-cancer bioactive peptide (ACBP) inhibits the initiation and progression of gastric cancer through apoptosis and cell cycle arrest, yet the mechanisms remain unclear. To elucidate the relationships between the effects of ACBP and the levels of cell differentiation, as well as the functional mechanisms of ACBP, we conducted a study using three human gastric cancer cell lines: NCI-N87, MGC-803, and another unspecified line. - Source: PubMed
Suyila QimugeLi XianSu Xiulan - The TP53 family of transcription factors plays key roles in driving development and combating cancer by regulating gene expression. TP53, TP63, and TP73-the three members of the TP53 family-regulate gene expression by binding to their DNA binding sites, many of which are situated within nucleosomes. To thoroughly examine the nucleosome-binding abilities of the TP53 family, we used Pioneer-seq, a technique that assesses a transcription factor's binding affinity to its DNA-binding sites at all possible positions within the nucleosome core particle. Using Pioneer-seq, we analyzed the binding affinities of TP53, TP63, and TP73 to 10 TP53 family binding sites across the nucleosome core particle. We find that the affinities of TP53, TP63, and TP73 for nucleosomes are primarily determined by the positioning of TP53 family binding sites within nucleosomes; TP53 family members bind strongly to the more accessible edges of nucleosomes but weakly to the less accessible centers of nucleosomes. Our results further show that the DNA-helical orientation of TP53 family binding sites within nucleosomal DNA impacts the nucleosome-binding affinities of TP53 family members, with binding-site composition impacting the affinity of each TP53 family member only when the binding-site location is accessible. Taken together, our results show that the accessibility, composition, and helical orientation of TP53 family binding sites collectively determine the nucleosome-binding affinities of TP53, TP63, and TP73. These findings help explain the rules underlying TP53 family-nucleosome binding and thus provide requisite insight into how we may better control gene expression changes involved in development and tumor suppression. - Source: PubMed
Publication date: 2025/03/18
Wilson Patrick DYu XinyangHandelmann Christopher RBuck Michael J - Here, we investigated the potential interaction between bromodomain-containing protein 4 (BRD4), an established epigenetic modulator and transcriptional coactivator, and p63, a member of the p53 transcription factor family, essential for epithelial development and skin homeostasis. Our protein-protein interaction assays demonstrated a strong and conserved physical interaction between BRD4 and the p53 family members-p63, p73, and p53-suggesting a shared binding region among these proteins. While the role of BRD4 in cancer development through its interaction with p53 has been explored, the effects of BRD4 and Bromodomain and Extra Terminal (BET) inhibitors in non-transformed cells, such as keratinocytes, remain largely unknown. Our functional analyses revealed changes in cellular proliferation and differentiation in keratinocytes depleted of either p63 or BRD4, which were further supported by using the BRD4 inhibitor JQ1. Transcriptomic analyses, chromatin immunoprecipitation, and RT-qPCR indicated a synergistic mechanism between p63 and BRD4 in regulating the transcription of keratinocyte-specific p63 target genes, including HK2, FOXM1, and EVPL. This study not only highlights the complex relationship between BRD4 and p53 family members but also suggests a role for BRD4 in maintaining keratinocyte functions. Our findings pave the way for further exploration of potential therapeutic applications of BRD4 inhibitors in treating skin disorders. - Source: PubMed
Publication date: 2024/11/27
Foffi EViolante APecorari RLena A MRugolo FMelino GCandi E