HNRPH1 Blocking Peptide
- Known as:
- HNRPH1 Blocking Peptide
- Catalog number:
- 33r-2975
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- HNRPH1 Blocking Peptide
Related genes to: HNRPH1 Blocking Peptide
- Gene:
- HNRNPH1 NIH gene
- Name:
- heterogeneous nuclear ribonucleoprotein H1
- Previous symbol:
- HNRPH1
- Synonyms:
- hnRNPH
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2017-01-12
Related products to: HNRPH1 Blocking Peptide
Related articles to: HNRPH1 Blocking Peptide
- Small Nuclear Ribonucleoprotein Polypeptide A (SNRPA), an RNA-binding protein associated with HCC survival, emerges as a key regulator requiring mechanistic study. - Source: PubMed
Publication date: 2026/05/01
Chang QingyaoWang YidiXu Jun - Alzheimer's disease (AD) is a neurodegenerative disorder associated with cognitive decline. Pathologically, AD is characterized by the accumulation of amyloid β (Aβ) monomers that may generate oligomers or fibrils in the extracellular space and inside the neurons. With time, the oligomers and fibrils aggregate into insoluble plaques, which may trigger a cascade of molecular events. These include altering gene expression at a broader level, implicating cross-talk with the nuclear machinery, including transcription. There is now emerging evidence implicating the role of RNAs and other nuclear proteins in AD pathogenesis, especially those associated with RNA splicing and ribonucleoproteins, which, along with post-transcriptional modifications, give rise to multiple functional proteoforms. Notably, RBPs themselves exist as multiple proteoforms, adding complexity to the proteome involved in AD. Therefore, in this review, we limit the discussion to the canonical protein forms of RBPs already established to have some role in AD pathophysiology. Recently, our proteomic study identified three such RBPs (SRSF2, hnRNPH1, and hnRNPA2B1) copurifying with amyloid, suggesting a possible interaction with Aβ and contribution to AD pathology. SRSF2 is a splicing factor involved in tau exon splicing, while hnRNPH1 and hnRNPA2B1 are both heterogeneous nuclear RBPs (hnRNPs) involved in mRNA processing. Some of the other hnRNPs have previously been implicated in AD and tau pathology. This review focuses on some of the recent evidence that suggests a possible involvement of RNA-associated nuclear proteins in dysregulation of widespread RNA processing affecting the AD pathogenesis pathways. We discuss how their dysfunction could modulate Aβ and tau-associated changes with an emphasis on understanding the linkage between nuclear RNA machinery and AD pathophysiology. Understanding this crosstalk may offer new insights into our understanding of AD and could provide RNA-centric therapeutic avenues. - Source: PubMed
Publication date: 2026/04/20
Kumar SandeepUpadhyay Arun - Mutations in cause an X-linked disorder characterized by developmental delay, intellectual disability, motor and gait disturbances, and seizures. Murine models that reproduce key clinical features of -related neurodevelopmental disorder suggest that it may result from a toxic gain of function of the mutant protein or a complex loss of normal HNRNPH2 function with impaired compensation by its paralog, HNRNPH1. In this study, we tested gapmer antisense oligonucleotides (ASOs) that target murine in a non-allele-specific manner. The lead ASO reduced messenger RNA (mRNA) and protein expression while inducing compensatory up-regulation of expression in both wild-type and mutant mouse brains. A single intracerebroventricular injection of the ASO into neonatal mutant mice rescued molecular and audiogenic seizure phenotypes and improved certain motor and cognitive phenotypes. ASO treatment at the juvenile stage also rescued audiogenic seizures. In contrast, ASO administration did not alter survival, body weight, or the incidence of hydrocephalus. In human induced pluripotent stem cell-derived neurons, a human-specific research ASO reduced mRNA and up-regulated mRNA. Mechanistically, we found that expression is regulated by alternative splicing and that HNRNPH2 modulates this process. These findings provide a preclinical proof of concept for ASO therapy and offer insights into its underlying molecular mechanism. - Source: PubMed
Publication date: 2026/04/22
Korff AneYang XiaojingOzdemir OzanSamanta AnanyaWang Yong-DongPatni TusharLavado Alfonso JKavirayani Anoop MurthyOchaba JosephPowers BeritBennett C FrankKim Hong JooTaylor J Paul - Coexisting myocardial infarction (MI) and type 2 diabetes mellitus (T2DM) is a common condition. We aimed to investigate the association between MI and type 2 diabetes (T2D) with mitophagy-related differentially expressed genes (MRDEGs) and the impact thereof on disease progression. - Source: PubMed
Publication date: 2026/04/08
Yang YingWan FeiyanXu XuelianXu WeiJiang LingliPan Pei - Although glioblastoma (GBM) harbors multiple genetic abnormalities leading to cell cycle deregulation, a functional mitotic checkpoint is essential to prevent mitotic catastrophe and tumor cell death. Here, we identify the RNA-binding protein HNRNPH1 as a key post-transcriptional modulator of G2/M checkpoint-associated genes in GBM. HNRNPH1 is overexpressed in malignant cells, especially in the neural- and oligodendrocyte-progenitor-like state, and its expression levels are higher in non-hypoxic regions of the tumor. Knocking out HNRNPH1 causes aberrant splicing and downregulation of several genes involved in cell division. These molecular alterations are associated with G2/M cell cycle arrest, reduced cell proliferation, abnormal cell morphology, and increased nuclear fragmentation. Silencing HNRNPH1 in vivo inhibits the tumor growth of patient-derived GBM cell-originated intracranial xenografts and has significant survival benefits. Together, our results show the critical importance of HNRNPH1 in cell cycle progression and tumor growth, potentially impacting the development of novel strategies to treat GBM. - Source: PubMed
Publication date: 2026/03/24
Villa Genaro RAlimonti PaoloToker Joseph SPiranlioglu RaziyeKarkoski Mikayla AMazzetti DeboraBen Mrid RedaEl Guendouzi SaraLauinger AlexaChiocca Andrew NEl Fatimy RachidChiocca E AntonioMineo Marco