PIH1D1 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- PIH1D1 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100663
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PIH1D1 antibody Polyclonal Antibodies Primary antibodies
Related genes to: PIH1D1 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- PIH1D1 NIH gene
- Name:
- PIH1 domain containing 1
- Previous symbol:
- NOP17
- Synonyms:
- FLJ20643, Pih1
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-30
- Date modifiied:
- 2018-06-05
Related products to: PIH1D1 antibody Polyclonal Antibodies Primary antibodies
Related articles to: PIH1D1 antibody Polyclonal Antibodies Primary antibodies
- The functional versatility of Hsp90 relies on its association with specialized co-chaperones that regulate client recruitment and maturation. Among these, the R2TP complex, comprising RUVBL1, RUVBL2, RPAP3 (Tah1 in yeast), and PIH1D1, acts as a conserved assembly factor essential for the biogenesis of large multiprotein machineries, including RNA polymerases, snoRNPs, PIKKs, and mTOR signaling complexes. RPAP3 functions as a central scaffold within the R2TP-Hsp90 system, linking Hsp90 and Hsp70 to the RUVBL1/2 ATPase core through its TPR domains and C-terminal interaction with PIH1D1. This modular organization enables RPAP3 to integrate chaperone-mediated folding with client delivery and complex assembly. Notably, dysregulation of RPAP3 has been implicated in oncogenic processes, highlighting its biomedical relevance. This review synthesizes current structural, functional, and evolutionary insights into RPAP3, focusing on its role within the R2TP-Hsp90 machinery and its emerging connections to human disease. - Source: PubMed
Publication date: 2026/04/09
Antonio Larissa MRamos Carlos H I - - Source: PubMed
Publication date: 2026/03/16
Pemberton Chris J - Anthracyclines, key chemotherapy agents, pose cardiotoxicity risks. In a 3-year study of 89 breast cancer patients treated with doxorubicin or epirubicin, more than 50% showed reduced left ventricular ejection fraction and progressive ventricular dilation. Although troponin-I flagged acute damage, it failed to predict long-term remodeling. Using a human methylome atlas, researchers identified 33 heart-specific methylated CpG sites and validated methylated PIH1D1 (mPIH1D1) as a novel biomarker. Elevated mPIH1D1 levels strongly correlated with ventricular dilation but not left ventricular ejection fraction decline, indicating its sensitivity to early cardiac remodeling. mPIH1D1 may complement troponin-I in risk assessment and cardiotoxicity management for patients undergoing anthracycline-based chemotherapy. - Source: PubMed
Publication date: 2026/03/11
Hsu Po-YenHuang Wan-HongLee Yi-YunPassier RobertLi Szu-ChinHong Chong-LinHung Shih-KaiLin Hong-YiLin Chun-HungChien Chen-YuLi Yi-DaLee Hsiang-ChunDésaubry LaurentNebigil Canan GChan Michael W Y - Human papillomaviruses (HPVs), particularly types 16 and 18, are major contributors to cervical cancer through the oncogenic activities of the E6 and E7 proteins. These viral proteins inactivate the tumour suppressors p53 and pRB, driving uncontrolled cellular proliferation. In this study, we investigated the interaction between the HPV E7 protein and the R2TP complex, a co-chaperone involved in essential cellular functions, including ribosome biogenesis, transcription, and macromolecular assembly. We identified PIH1D1, a core R2TP subunit, as an interacting partner of HPV16 and HPV18 E7 proteins. Mutagenesis and pull-down assays showed that phosphorylation of HPV E7 by casein kinase 2 (CK2) is critical for this interaction, as mutations of serine residues within the CK2 phospho-acceptor site on E7 disrupted the binding with PIH1D1. Furthermore, PIH1D1 facilitated the association of E7 with the retinoblastoma protein (pRB), forming a complex that likely promotes cancer cell proliferation. Immunohistochemical analysis of cervical cancer tissues revealed overexpression of PIH1D1, RUVBL1, and RPAP3-key components of the R2TP complex. Functional assays confirmed that PIH1D1 is crucial for cervical cancer cell growth and migration, as its silencing reduced E7 stability and impaired proliferation. Collectively, these findings highlight that PIH1D1, and by extension, the R2TP complex, is integral to the HPV-driven malignancy and suggest potential as therapeutic targets in HPV-related cancers. IMPORTANCE: Despite being largely preventable through vaccination, cervical cancer is a significant concern for public health. Research is essential to understand the factors contributing to its high incidence and mortality and to devise effective prevention and treatment strategies. We investigated the functional role of PIH1D1, a core subunit of the R2TP complex, in the HPV-mediated cervical carcinogenesis. The interaction of the R2TP complex, HPV E7, and the tumour suppressor pRB proteins may be essential in driving malignant transformation. - Source: PubMed
Publication date: 2026/03/05
Shadang MahaiwonArumugam ArunaSingh Dhiraj KumarKeshari PankajMathur SandeepIyer Venkateswaran KSinghal SeemaChauhan Shyam SAkhter QulsumMir Riyaz Ahmad - The PAQosome (R2TP/PFDL complex) is a recently characterized co-chaperone of Hsp90 that orchestrates the assembly and stabilization of diverse macromolecular protein complexes essential for cellular homeostasis. It consists of RUVBL1, RUVBL2, PIH1D1, RPAP3 and a PFDL module consisting of prefoldin and prefoldin-like proteins. RPAP3 and PIH1D1 are subunits exclusively for the R2TP complex, and they act as central adaptors through their interactions with RUVBL1/2, Hsp90 and clients. Originally described in the context of ribonucleoprotein and PIKK assembly, evolving evidence now implicates PIH1D1 and RPAP3 in a broad spectrum of biological processes, including ciliogenesis, RNA silencing, DNA damage response, metabolic regulation, and oncogenesis. The mechanistic basis of substrate recognition, the phosphorylation-independent interactions, and the functional contribution of alternative PAQosome assemblies remain limited. This review highlights PIH1D1 and RPAP3 as dynamic proteins at the crossroads of protein homeostasis, signaling pathways, and diseases. - Source: PubMed
Publication date: 2025/12/21
Shadang MahaiwonAhmad Mir Riyaz