PRDM2 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- PRDM2 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100514
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PRDM2 antibody Polyclonal Antibodies Primary antibodies
Ask about this productRelated genes to: PRDM2 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- PRDM2 NIH gene
- Name:
- PR/SET domain 2
- Previous symbol:
- -
- Synonyms:
- RIZ, RIZ1, RIZ2, KMT8, MTB-ZF, HUMHOXY1, KMT8A
- Chromosome:
- 1p36.21
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-23
- Date modifiied:
- 2016-11-03
Related products to: PRDM2 antibody Polyclonal Antibodies Primary antibodies
Related articles to: PRDM2 antibody Polyclonal Antibodies Primary antibodies
- PRDM2 is a histone methyltransferase that regulates gene expression through histone H3 lysine 9 methylation. It is involved in the DNA damage response by controlling chromatin remodeling and maintaining genomic integrity. However, the functional relevance of its phosphorylation remains poorly understood. To address this gap, we systematically characterized PRDM2 phosphosites and their associated phospho-signaling networks using large-scale cellular phosphoproteomics data curated from PubMed-indexed articles. Frequency-based ranking revealed Ser643 and Ser421 as predominant phosphosites, detected across 334 and 141 qualitative datasets and 70 and 47 differential cellular phosphoproteomics datasets, respectively. To explore PRDM2-associated phospho-signaling, expression co-regulation analysis was performed to identify phosphosites in other proteins exhibiting consistently similar or opposing expression patterns relative to the predominant PRDM2 phosphosites. This analysis identified 1,251 phosphosites in other proteins showing high-confidence expression co-regulation with PRDM2 Ser421 and 715 phosphosites with PRDM2 Ser643. Functional enrichment revealed significant associations with cell cycle regulation, chromatin organization, RNA processing, and DNA damage response (DDR) pathways. Notably, phosphosites in 30 DDR-related proteins positively co-regulated with Ser643 and 28 with Ser421. Additionally, ATR was identified as a potential kinase predicted to phosphorylate the predominant PRDM2 sites, and its phosphosites exhibited consistent expression co-regulation with PRDM2 sites. Collectively, this study establishes a comprehensive phospho-signaling framework for PRDM2, uncovering its strong association with DNA damage response pathways and providing mechanistic insights into its regulatory network. Clinical trial registration: This study is not part of any clinical trial. - Source: PubMed
Publication date: 2026/05/20
Gopalakrishnan VaishnaviMahin AlthafDcunha LeonaGopalakrishnan Athira PerunellyGeorge MejoJohn LevinShivamurthy Prathik BasthikoppaUmmar SamseeraVattoth Nazah NaurahRaju Rajesh - TAR DNA-binding protein 43 (TDP-43) proteinopathy is a central hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), yet current experimental models fail to reproduce the full pathological spectrum without external stress or TDP-43 overexpression. This study aims to establish a human induced pluripotent stem cells (iPSC)-derived system that spontaneously manifests TDP-43 pathology driven by an ALS-associated TDP-43 mutation. - Source: PubMed
Publication date: 2025/11/10
Zhang QiLiu MengFan XiaojuanChin NatalieXu YueSuh JessicaAmniouel SoukainaLinask KaariZou JizhongHafner MarkusMa LichunZheng WeiYe Yihong - Lung cancer is the leading cause of tumor-related deaths worldwide. In over 70 % of patients, the positive regulatory domain 2 (PRDM2) gene, which encodes the tumor suppressor RIZ1 and the oncogenic RIZ2 isoforms, is dysregulated, promoting tumor progression via RIZ2 overexpression. In this study, we used ARIZ-047, a siRNA designed to inhibit the effect of the oncogenic protein RIZ2 selectively. Inhibiting RIZ2 with ARIZ-047 treatment increased RIZ1 expression and decreased the viability of a lung cancer cell line (A549). Transcriptomic analysis after ARIZ-047 treatment revealed the modulation of the Wnt signaling pathway and downregulation of genes associated with proliferation and metastasis. In vivo, ARIZ-047 encapsulated in targeted nanoparticles (T-CaP) showed a marked reduction in tumor size and RIZ2 expression in a xenograft mouse model. In conclusion, this study identifies ARIZ-047 as a targeted therapy in lung cancer, which inhibits RIZ2 explicitly and suggests the role of the Wnt signaling pathway in RIZ2 overexpression. - Source: PubMed
Publication date: 2025/11/23
Kumar SanjayMalik Md ZubbairChaturvedi MayaMishra MohitDi Donato MarziaCasamassimi AmeliaAbbondanza CiroGazzerro PatriziaNguyen ChuongNuñez Nicole NSen SomduttaNiles BradChaturvedi Rupesh - PR/SET domain 2 (PRDM2)/RIZ is a member of the histone/protein methyltransferases (PRDMs) superfamily. Discovered to have the ability to bind retinoblastoma in the mid-1990s, PRDM2 was assumed to play a role in neuronal development. Like other family members characterized by a conserved N-terminal PR structural domain and a classical C2H2 zinc-finger array at the C-terminus, PRDM2 encodes two major protein types, the RIZ1 and RIZ2 isoforms. The two subtypes differ in the presence or absence of the PR domain: the RIZ1 subtype has the PR domain, whereas the RIZ2 subtype lacks it. The PR domain exhibits varying conservation levels across species and shares structural and functional similarities with the catalytic SET domain, defining histone methyltransferases. Functioning as an SET domain, the PR domain possesses protein-binding interfaces and acts as a lysine methyltransferase. The variable number of classic C2H2 zinc fingers at the C-terminus may mediate protein-protein, protein-RNA, or protein-DNA interactions. An imbalance in the RIZ1/RIZ2 mechanism may be an essential cause of malignant tumors, where PR-positive isoforms are usually lost or downregulated. Conversely, PR-negative isoforms are always present at higher levels in cancer cells. RIZ1 isoforms are also important targets for estradiol interaction with hormone receptors. PRDM2 can regulate gene transcription and expression combined with transcription factors and plays a role in the development of several systemic diseases through mRNA expression deletion, code-shift mutation, chromosomal deletion, and missense mutation occurrence. Thus, PRDM2 is a key indicator for disease diagnosis, but it lacks systematic summaries to serve as a reference for study. Therefore, this paper describes the structure and biological function of PRDM2 from the perspective of its role in various systemic diseases. It also organizes and categorizes its latest research progress to provide a systematic theoretical basis for a more in-depth investigation of the molecular mechanism of PRDM2's involvement in disease progression and clinical practice. - Source: PubMed
Publication date: 2025/08/15
Deng ShiqiLi HuiZhu ChenyuZhang LingliZou Jun - To explore whether micro ribonucleic acid (miR)-153 regulates positive regulatory/SET domain 2 (PRDM2) in a targeted manner and affects the proliferation and apoptosis of non-small cell lung cancer (NSCLC) A549 cells. - Source: PubMed
Chen JiXie ShiliangFeng MiaoWang Dan