TRIP13 antigen

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636.35 €

Known as:: TRIP13 antigenic
Catalog number:: 'H00009319-P01-10
Product Quantity:: 10
Category:: -
Supplier:: ACR
Gene target:: TRIP13 antigen

Related genes to: TRIP13 antigen

Gene:: TRIP13 ^{NIH gene}
Name:: thyroid hormone receptor interactor 13
Previous symbol:: -
Synonyms:: 16E1BP
Chromosome:: 5p15.33
Locus Type:: gene with protein product
Date approved:: 2000-01-04
Date modifiied:: 2016-10-05

Related products to: TRIP13 antigen

Related articles to: TRIP13 antigen

RRM2 as a biomarker and therapeutic target in letrozole resistant estrogen receptor positive breast cancer.
Letrozole is a first-line aromatase inhibitor for estrogen receptor-positive (ER +) breast cancer, yet resistance occurs in 20-30% of patients, significantly limiting therapeutic benefit. The absence of reliable pretreatment biomarkers remains a major barrier to precision therapy. This study aimed to identify robust prognostic biomarkers and elucidate molecular mechanisms underlying letrozole resistance through integrative bioinformatics, molecular docking, and cell-based functional assays. Weighted gene co-expression network analysis of transcriptomic datasets revealed a module strongly associated with nonresponse. From this, seven candidate genes (BUB1B, CENPU, KIF11, RRM2, NUSAP1, TRIP13, PRC1) were identified as significantly overexpressed in tumors and consistently correlated with poor survival in ER + breast cancer. Among them, RRM2 emerged as the most clinically relevant marker. Molecular docking demonstrated a potential competitive interaction between RRM2 and letrozole, implicating disruption of aromatase inhibition and DNA replication pathways in resistance, while functional assays in ER + cell lines showed that RRM2 modulates proliferation and MYC-CCND1 signaling. Validation in an independent letrozole-treated cohort confirmed the strong prognostic value of RRM2. These findings provide novel mechanistic insights into endocrine resistance and establish RRM2 as a pivotal prognostic biomarker and therapeutic target. This work offers a strong foundation for biomarker-guided strategies to optimize treatment and overcome resistance in ER + breast cancer. - Source: PubMed
Publication date: 2026/05/21
Hung Wan-YuHuang Shih-ChunChen Shou-TungLin Chi-ChenHou Ming-Hon
Multi-omics analysis and functional validation reveal the oncogenic role of TRIP13.
Thyroid hormone receptor-interacting protein 13 (TRIP13), an enzyme from the AAA-ATPase family, facilitates the assembly or disassembly of protein complexes and participates in various biological processes. However, its impact on cancer immune infiltration and pan-cancer prognosis remains largely unexplored. - Source: PubMed
Publication date: 2026/04/22
Zhao YuanqiaoZhao YongqiLiu RuilinLi JingWang Yinhuai
The synaptonemal complex: structure, function, and clinical implications†.
The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy
Genotoxic effects of 6PPD-quinone on juvenile European seabass (Dicentrarchus labrax): Impacts on DNA replication fidelity and oxidative DNA damage.
Juvenile European seabass (Dicentrarchus labrax) were exposed to environmentally relevant 6PPD-quinone (2.85 µg/L) for five days to evaluate transcriptional, oxidative, and antioxidant responses and histopathology. The liver showed the strongest gene induction: cdc28 (∼75×), bax (48×), spc25 (45×), and hsp70 (42.5×). Kidney responses were moderate, with bax up ∼5.5× and hsp70 and casp9 ∼2×, while pcna, cenpi, cenpf, and cdc28 were downregulated (0.32-0.66×). Spleen and intestine exhibited marked upregulation of spc25, cenpf, cenpi, and bcl2 (up to ∼34.6× and 16×, respectively), whereas trip13, bax, and bcl2 were unchanged in spleen. Gills displayed strong trip13 (∼32.5×) and spc25 (∼13.7×) induction but downregulation of bax and bcl2. Oxidative DNA damage (8-OHdG) increased in all organs except skin, peaking in spleen; N-myc protein rose in spleen. Catalase activity decreased in liver, kidney, and skin but increased in spleen; MDA decreased in most tissues except skin. Histopathology revealed multifocal hepatic necrosis and vacuolation, splenic fibrosis with hemorrhage and lymphoid depletion, intestinal villous sloughing with submucosal inflammation, severe myositis, epidermal desquamation, and gill lamellar damage. In conclusion, short-term exposure to environmentally relevant 6PPD-quinone elicits organ-specific molecular, oxidative, and pathological alterations in juvenile seabass, indicating significant multisystemic toxicity and potential population-level risks and warrants further ecological investigation. - Source: PubMed
Publication date: 2026/04/19
Abo-Al-Ela Haitham GAl Wakeel Rasha AZaki Abeer GamalElkatatny Nasema MahmoudAbdelatty AlaaAssas MonaZaid Attia A AbouElnaggar Mahmoud MAbdo Safaa E
Dual Inhibition of TRIP13 and Aurora A Induces Mitotic DNA Damage and Concurrent Pyroptotic-apoptotic Cell Death in Rb-deficient Cancer Cells.
Cancers driven by a loss of tumor suppressor function lack actionable druggable targets. We investigated the cell cycle-specific mechanisms underlying the efficacy of co-targeting TRIP13 and Aurora A by defining their key functions in Rb-deficient cancers to develop effective treatment strategies. - Source: PubMed
Publication date: 2026/04/21
Yapindi LacinGhosh SomaShen LiDiao LixiaWang JingJohnson Faye M

TRIP13 antigen

Related genes to: TRIP13 antigen

Related products to: TRIP13 antigen

Related articles to: TRIP13 antigen

RRM2 as a biomarker and therapeutic target in letrozole resistant estrogen receptor positive breast cancer.

Multi-omics analysis and functional validation reveal the oncogenic role of TRIP13.

The synaptonemal complex: structure, function, and clinical implications†.

Genotoxic effects of 6PPD-quinone on juvenile European seabass (Dicentrarchus labrax): Impacts on DNA replication fidelity and oxidative DNA damage.

Dual Inhibition of TRIP13 and Aurora A Induces Mitotic DNA Damage and Concurrent Pyroptotic-apoptotic Cell Death in Rb-deficient Cancer Cells.