SF3B14 Blocking Peptide
- Known as:
- SF3B14 Blocking Peptide
- Catalog number:
- 33r-3788
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- SF3B14 Blocking Peptide
Ask about this productRelated genes to: SF3B14 Blocking Peptide
- Gene:
- SF3B6 NIH gene
- Name:
- splicing factor 3b subunit 6
- Previous symbol:
- -
- Synonyms:
- P14, SF3B14a, Ht006, CGI-110, SAP14a
- Chromosome:
- 2p23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2014-02-14
- Date modifiied:
- 2016-10-05
Related products to: SF3B14 Blocking Peptide
Related articles to: SF3B14 Blocking Peptide
- SF3B6 functions as a splicing factor, and is closely associated with the malignant progression of multiple cancer types, including breast cancer. However, its underlying mechanism is largely unknown in breast tumor cells. In this study, we investigated the molecular mechanism and downstream targets of SF3B6 by transfecting the siRNA of SF3B6 (siSF3B6) into MDA-MB-231 cells and combining with high-throughput transcriptome sequencing (RNA-seq) and improved RNA immunoprecipitation sequencing (iRIP-seq) technology. We found siSF3B6 significantly repressed cellular proliferation and migration levels, but increased apoptosis levels of MDA-MB-231 cells. Downstream RNA-seq analysis revealed that SF3B6 silencing resulted in widespread changes in differentially expressed genes (DEGs) and regulatory alternative splicing events (RASEs) that were involved in inflammatory response and immune regulatory pathways, such as the NF-κB signaling pathway. The iRIP-seq analysis indicated that SF3B6 can regulate the gene expression and alternative splicing profile by directly interacting with its targeting mRNAs. Further analysis showed that SF3B6 potentially contributes to the malignant properties of TNBC by regulating the expression and splicing of key oncogenes, including PPM1F and FASN, and tumor suppressor genes, including RLF and RECQL4, which were validated by RT-qPCR experiment. In summary, this study highlights the crucial molecular role of SF3B6 in breast cancer cells, providing new insights into its potential as a biomarker or valuable target in breast cancer diagnosis and treatment in future. - Source: PubMed
Publication date: 2025/11/13
Yuan ChunxiuGao YuanyuanHuang YingZhao YanjiaoLi XuanWang NanWang Sheng - Splicing factor 3b subunit 6(SF3B6), a subunit of the SF3B complex, regulates the process of RNA splicing by recognizing the branch point adenosine in pre-mRNA and facilitating the interaction between U2 snRNA and the branch point sequence. Currently, there is no systematic multi-omics study exploring the diagnostic, prognostic, and immunotherapy predictive value of SF3B6 in pan-cancer, nor is its role in hepatocellular carcinoma (HCC) clear. - Source: PubMed
Publication date: 2025/04/28
Tu LinshuangLuo JiefuYin YaYu Huihong - The European flounder is readily chosen as an experimental subject and model in physiological and ecotoxicological studies mostly because of its adaptability to laboratory conditions. Many studies utilise a quantitative PCR (qPCR) approach to ascertain the expression of target genes under experimental conditions. Such an approach relies heavily on the selection of reference genes with stable expression. Yet certain housekeeping genes are commonly used in this role, often without due consideration of their overall expression patterns. Therefore, new approaches should be developed to identify stable reference genes for a given species and to expand the general pool of genes suitable for the reference in qPCR analysis. - Source: PubMed
Publication date: 2024/11/21
Pomianowski KonradBurzyński Artur - The B complex is a key intermediate stage of spliceosome assembly. To improve the structural resolution of monomeric, human spliceosomal B (hB) complexes and thereby generate a more comprehensive hB molecular model, we determined the cryo-EM structure of B complex dimers formed in the presence of ATP S. The enhanced resolution of these complexes allows a finer molecular dissection of how the 5' splice site (5'ss) is recognized in hB, and new insights into molecular interactions of FBP21, SNU23 and PRP38 with the U6/5'ss helix and with each other. It also reveals that SMU1 and RED are present as a heterotetrameric complex and are located at the interface of the B dimer protomers. We further show that MFAP1 and UBL5 form a 5' exon binding channel in hB, and elucidate the molecular contacts stabilizing the 5' exon at this stage. Our studies thus yield more accurate models of protein and RNA components of hB complexes. They further allow the localization of additional proteins and protein domains (such as SF3B6, BUD31 and TCERG1) whose position was not previously known, thereby uncovering new functions for B-specific and other hB proteins during pre-mRNA splicing. - Source: PubMed
Publication date: 2024/02/21
Zhang ZhenweiKumar VinayDybkov OlexandrWill Cindy LUrlaub HenningStark HolgerLührmann Reinhard - The SF3B splicing complex is composed of SF3B1-6 and PHF5A. We report a developmental disorder caused by de novo variants in PHF5A. - Source: PubMed
Publication date: 2023/07/06
Harms Frederike LDingemans Alexander J MHempel MajaPfundt RolphBierhals TatjanaCasar ChristianMüller ChristianNiermeijer Jikke-Mien FFischer JanJahn ArneHübner ChristophMajore SilviaAgolini EmanueleNovelli Antoniovan der Smagt JasperErnst Robertvan Binsbergen EllenMancini Grazia M Svan Slegtenhorst MarjonBarakat Tahsin StefanWakeling Emma LKamath ArveenDownie LilianPais LynnWhite Susan Mde Vries Bert B AKutsche Kerstin