Recombinant Human TAF15 Protein Catalog Number: ATGP2466

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Recombinant human TAF15 protein Catalog Number: ATGP2466 PRODUCT INPORMATION Expression system E.coli Domain 148-406aa UniProt No. Q92804 NCBI Accession No. NP_631961 Alternative Names TATA-binding protein-associated factor 2N isoform 1, TATA-binding protein-associated factor 2N isoform 1, Npl3, RBP56, TAF2N, TAFII68 PRODUCT SPECIFICATION Molecular Weight 30kDa (282aa) confirmed by MALDI-TOF Concentration 0.25mg/ml (determined by Bradford assay) Formulation Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 30% glycerol, 1mM DTT Purity > 90% by SDS-PAGE Tag His-Tag Application SDS-PAGE Storage Condition Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles. BACKGROUND Description TAF15 is a member of the TET family of RNA-binding proteins. The encoded protein plays a role in RNA polymerase II gene transcription as a component of a distinct subset of multi-subunit transcription initiation factor TFIID complexes. Translocations involving this gene play a role in acute leukemia and extraskeletal myxoid chondrosarcoma, and mutations in this gene may play a role in amyotrophic lateral sclerosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. 1 Recombinant human TAF15 protein Catalog Number: ATGP2466 Recombinant human TAF15 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques. Amino acid Sequence MGSSHHHHHH SSGLVPRGSH MGSSYHSQRE NYSHHTQDDR RDVSRYGEDN RGYGGSQGGG RGRGGYDKDG RGPMTGSSGG DRGGFKNFGG HRDYGPRTDA DSESDNSDNN TIFVQGLGEG VSTDQVGEFF KQIGIIKTNK KTGKPMINLY TDKDTGKPKG EATVSFDDPP SAKAAIDWFD GKEFHGNIIK VSFATRRPEF MRGGGSGGGR RGRGGYRGRG GFQGRGGDPK SGDWVCPNPS CGNMNFARRN SCNQCNEPRP EDSRPSGGDF RGRGYGGERG YR General References Martini A, La Starza R, et al. (2002). Cancer Res. 62(19):5408-12. DATA SDS-PAGE 3ug by SDS-PAGE under reducing condition and visualized by coomassie blue stain. 2.

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TAF15 Is Important for Cellular Proliferation and Regulates the Expression of a Subset of Cell Cycle Genes Through Mirnas
Oncogene (2013) 32, 4646–4655 & 2013 Macmillan Publishers Limited All rights reserved 0950-9232/13 www.nature.com/onc ORIGINAL ARTICLE TAF15 is important for cellular proliferation and regulates the expression of a subset of cell cycle genes through miRNAs M Ballarino1, L Jobert1,4, D Dembe´le´ 1, P de la Grange2, D Auboeuf3 and L Tora1 TAF15 (formerly TAFII68) is a member of the FET (FUS, EWS, TAF15) family of RNA- and DNA-binding proteins whose genes are frequently translocated in sarcomas. By performing global gene expression profiling, we found that TAF15 knockdown affects the expression of a large subset of genes, of which a significant percentage is involved in cell cycle and cell death. In agreement, TAF15 depletion had a growth-inhibitory effect and resulted in increased apoptosis. Among the TAF15-regulated genes, targets of microRNAs (miRNAs) generated from the onco-miR-17 locus were overrepresented, with CDKN1A/p21 being the top miRNAs- targeted gene. Interestingly, the levels of onco-miR-17 locus coded miRNAs (miR-17-5p and miR-20a) were decreased upon TAF15 depletion and shown to affect the post-transcriptional regulation of TAF15-dependent genes, such as CDKN1A/p21. Thus, our results demonstrate that TAF15 is required to regulate gene expression of cell cycle regulatory genes post-transcriptionally through a pathway involving miRNAs. The findings that high TAF15 levels are needed for rapid cellular proliferation and that endogenous TAF15 levels decrease during differentiation strongly suggest that TAF15 is a key regulator of maintaining a highly proliferative rate of cellular homeostasis. Oncogene (2013) 32, 4646–4655; doi:10.1038/onc.2012.490; published online 5 November 2012 Keywords: FUS/EWS/TAF15 (FET) proteins; miRNAs; transcription; proliferation; neuronal differentiation; neuroblastoma INTRODUCTION possible role of TAF15 in additional steps of RNA metabolism.
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RNA Binding Protein TAF15 Suppresses Toxicity in a Yeast Model of FUS Proteinopathy
RNA Binding Protein TAF15 Suppresses Toxicity in a Yeast Model of FUS Proteinopathy Elliott Hayden Wright State University Aicha Kebe Wright State University Shuzhen Chen Wright State University Abagail Chumley Wright State University Chenyi Xia Shanghai University of Traditional Chinese Medicine Quan Zhong Wright State University Shulin Ju ( [email protected] ) Wright State University Research Article Keywords: FUS, RNA binding protein, ALS, toxicity Posted Date: April 22nd, 2021 DOI: https://doi.org/10.21203/rs.3.rs-437201/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License RNA binding protein TAF15 suppresses toxicity in a yeast model of FUS proteinopathy Elliott Hayden1, Aicha Kebe1, Shuzhen Chen1, Abagail Chumley1, Chenyi Xia2, Quan Zhong1* and Shulin Ju1* 1Department of Biological Sciences, Wright State University, Dayton, OH 45435 2School of Basic Medicine, Shanghai University of Traditional Medicine, Shanghai, China 201203 *Corresponding authors: [email protected]; [email protected] Abstract Mutations in Fused in Sarcoma (FUS), an RNA binding protein that functions in multiple steps in gene expression regulation and RNA processing, are known to cause familial amyotrophic lateral sclerosis (ALS). Since this discovery, mutations in several other RNA binding proteins (RBPs) have also been linked to ALS. Some of these ALS-associated RBPs have been shown to colocalize with ribonucleoprotein (RNP) granules such as stress granules and processing bodies (p-bodies). Characterization of ALS-associated proteins, their mis-localization, aggregation and toxicity in cellular and animal models have provided critical insights in disease. More and more evidence has emerged supporting a hypothesis that impaired clearance, inappropriate assembly, and dysregulation of RNP granules play a role in ALS.
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FUS ALS-Causative Mutations Impact FUS Autoregulation and the Processing of RNA-Binding Proteins Through Intron Retention
bioRxiv preprint doi: https://doi.org/10.1101/567735; this version posted March 4, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Humphrey et al. FUS ALS-causative mutations impact FUS autoregulation and the processing of RNA-binding proteins through intron retention 1,2,3# 1 2 2 1 Jack Humphrey , Nicol Birsa , Carmelo Milioto , David Robaldo , Matthew Bentham , 1,3 1 4 1,2,5 4,6 Seth Jarvis , Cristian Bodo , Maria Giovanna Garone , Anny Devoy , Alessandro Rosa , 4,6 1 2,5 1,7 Irene Bozzoni , Elizabeth Fisher , Marc-David Ruepp , Giampietro Schiavo , Adrian 1,2 3 1 Isaacs , Vincent Plagnol , Pietro Fratta 1. UCL Queen Square Institute of Neurology, University College London, London WC1E 6BT, UK. 2. UK Dementia Research Institute, London, UK 3. UCL Genetics Institute, University College London, London WC1E 6BT, UK. 4. Sapienza University of Rome, Rome, IT. 5. Maurice Wohl Clinical Neuroscience Institute, King’s College London, London, UK. 6. Center for Life Nano Science, Istituto Italiano di Tecnologia, Rome, IT. 7. Discoveries Centre for Regenerative and Precision Medicine, University College London Campus, London WC1N 3BG, UK. #. Current address: Ronald M. Loeb Center for Alzheimer’s Disease, Department of Neuroscience and Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY, 10129, USA. Key words: FUS, autoregulation, ALS, intron retention Correspondence: [email protected]; [email protected] Abstract Mutations in the RNA binding protein FUS cause amyotrophic lateral sclerosis (ALS), a devastating neurodegenerative disease in which the loss of motor neurons induces progressive weakness and death from respiratory failure, typically only 3-5 years after onset.
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RNA-Binding Proteins with Prion-Like Domains in Health and Disease
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