RRBP1 antibody (FITC) Polyclonal Antibodies Primary antibodies
- Known as:
- RRBP1 (anti-) (fluorecein) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb103423
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- RRBP1 antibody (FITC) Polyclonal Antibodies Primary antibodies
Related genes to: RRBP1 antibody (FITC) Polyclonal Antibodies Primary antibodies
- Gene:
- RRBP1 NIH gene
- Name:
- ribosome binding protein 1
- Previous symbol:
- -
- Synonyms:
- ES/130, hES
- Chromosome:
- 20p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-03-20
- Date modifiied:
- 2016-10-05
Related products to: RRBP1 antibody (FITC) Polyclonal Antibodies Primary antibodies
Related articles to: RRBP1 antibody (FITC) Polyclonal Antibodies Primary antibodies
- The EEF1B complex plays a central role in translation elongation by reactivating EEF1A for the delivery of aminoacyl-tRNAs to the ribosome. Among its components, EEF1D undergoes alternative splicing to produce one long and several short isoforms, each with distinct N-terminal domains and tissue-specific expression patterns. Although the short isoforms are broadly expressed, their physiological functions remain poorly characterized. In this study, we show that short EEF1D isoforms containing exon 5 interact with the ER-resident scaffold protein KTN1 and RRBP1, thereby anchoring the EEF1B complex to the ER. Mass spectrometry analyses of FLAG-tagged EEF1D identified these interactions, and deletion of exon 5 disrupted ER anchoring, resulting in diffuse cytoplasmic localization of the EEF1B complex. In exon 5 KO mice, this altered localization was accompanied by a reduction in EEF1B subunit abundance in multiple tissues, including the liver, although global protein synthesis rates remained unchanged. Together, these findings uncover an ER-anchoring mechanism controlled by alternative splicing that shapes the spatial organization and abundance of the elongation machinery in vivo. - Source: PubMed
Publication date: 2026/06/02
Jamous MuhammadHosogane MasakiHuang XiaoxinSuzuki MikikoHatano AtsushiShichino YuichiIwasaki ShintaroMurayama KazutakaMatsumoto MasakiNakayama Keiko - Acquired resistance to 5-fluorouracil (5-FU) is a primary clinical challenge in colorectal cancer (CRC) treatment. Our study aimed to identify key factors predictive of 5-FU resistance and to elucidate their functional mechanisms by combining multi-omics analysis with experimental verification. The prognostic model was constructed based on the gene expression omnibus (GEO, GSE196900, GSE166555) and the cancer genome atlas (TCGA)-Colon Adenocarcinoma (COAD) datasets combined with regression analysis. Kaplan-Meier (K-M), receiver operating characteristic (ROC) curve, and nomogram were used to evaluate the predictive performance of the prognostic model. Gene ontology (GO) and Kyoto encyclopedia of genes and genomes (KEGG) were used for functional enrichment analysis. Single-cell RNA sequencing (scRNA-seq, GSE166555) and qRT-PCR analysis were used to analyze the tumor microenvironment and gene expression. In cell experiments, CCK-8 assay measured IC value. Glycolysis metabolism was evaluated by detecting glucose consumption, lactic acid production, extracellular acidification rate (ECAR), and oxygen consumption rate (OCR); cell stemness was evaluated by sphere formation assay. A 5-gene prognostic model was successfully constructed, which could effectively distinguish the high-/low-risk groups of CRC patients and was significantly correlated with overall survival. Ribosome binding protein 1 (RRBP1) is highly expressed in cancer tissues of non-responders to chemotherapy. It is also highly expressed in tumor epithelial cells, and its high expression is closely related to aneuploidy characteristics, up-regulation of oncogenes, and activation of pro-survival pathways. In vitro experiments confirmed that knockdown of RRBP1 significantly enhanced the sensitivity of CRC cells to 5-FU and inhibited cell proliferation. Mechanistically, RRBP1 knockdown effectively reversed the enhanced glycolysis activity and stem cell-like properties of 5-FU-resistant cells. This study established RRBP1 as a key CRC prognostic factor and 5-FU resistance driver, operating through the regulation of cell glycolysis and stemness. RRBP1 emerges as a new biomarker and therapeutic target for predicting the efficacy of 5-FU. - Source: PubMed
Ge HuiXiao ZhengZheng PeimingZhou Chongmei - Osteoarthritis (OA) is a widespread chronic joint disorder characterized by progressive cartilage degeneration, leading to substantial impairment in quality of life for millions of individuals globally. Cellular senescence has been increasingly recognized as a central contributor to OA pathogenesis, with senescent chondrocytes exhibiting a senescence-associated secretory phenotype that promotes tissue destruction. Long non-coding RNAs (lncRNAs) are known to play essential roles in maintaining cartilage homeostasis; however, their regulatory functions in OA remain poorly defined. This study aimed to elucidate the expression patterns, biological roles, and molecular mechanisms of lncRNA HOXC-AS3 in chondrocyte physiology and OA development. - Source: PubMed
Publication date: 2026/02/15
Wang ChanZhou JunChen LuluMa ChangyanDong ZhanMiao Dengshun - Crosstalk between inflammation and the immune system plays an important role in tumor malignant progression, immune evasion, and immunotherapy efficacy. This study aims to explore the significance of inflammation-associated gene ribosomal-binding protein 1 (RRBP1) in modulating tumor malignant progression and immune escape. - Source: PubMed
Publication date: 2026/02/03
Shen ChengquanLiu ChangxueHu DingGe HuaixiLi ChengQin RuizeZhao XinzhaoWang YonghuaNiu Haitao - Peroxisomes are single-membrane-bound organelles essential for human health, yet the mechanisms of peroxisome biogenesis are not fully understood. Here using a systematic double screening approach, we identified ribosome-binding protein 1 (RRBP1) as a novel peroxisome biogenesis factor in human cells. Deletion of RRBP1 in HEK293T cells led to a reduction in both peroxisome number and peroxisomal protein levels as well as in defects in processing of peroxisomal matrix proteins, such as ACOX1 and thiolase. However, cell proliferation and protein translation were not altered in cells lacking RRBP1. RRBP1 depletion did not affect peroxisome-endoplasmic reticulum (ER) contact sites, and pexophagy did not contribute to the reduction of peroxisomes in RRBP1 knockout cells. Instead, in the absence of RRBP1, peroxisomal proteins were processed by proteasomal degradation, suggesting that RRBP1 plays a role in the insertion of these proteins into ER membranes and their stabilization. Altogether, our results show that RRBP1 promotes peroxisome biogenesis in human cells, highlighting the power of systematic approaches in discovering novel factors of organellar biogenesis. - Source: PubMed
Publication date: 2025/12/18
Fatima KaneezVihinen HelenaAkpinar AniSomborac TamaraPaatero AnjaJokitalo EijaPaavilainen VilleKatajisto PekkaKonovalova Svetlana