STAU1 Antibody / Staufen (R31848)

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STAU1 Antibody / Staufen (R31848) Catalog No. Formulation Size R31848 0.5mg/ml if reconstituted with 0.2ml sterile DI water 100 ug Bulk quote request Availability 1-3 business days Species Reactivity Human Format Antigen affinity purified Clonality Polyclonal (rabbit origin) Isotype Rabbit IgG Purity Antigen affinity Buffer Lyophilized from 1X PBS with 2.5% BSA and 0.025% sodium azide UniProt O95793 Localization Cytoplasmic Applications Western blot : 0.1-0.5ug/ml Limitations This STAU1 antibody is available for research use only. Western blot testing of human 1) PANC, 2) A549 and 3) 293 cell lysate with STAU1 antibody. Predicted molecular weight: ~55 kDa (short form) and 63 kDa (long form). Description Double-stranded RNA-binding protein Staufen homolog 1 is a protein that in humans is encoded by the STAU1 gene. Staufen is a member of the family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. The human homologue of staufen encoded by STAU, in addition contains a microtubule- binding domain similar to that of microtubule-associated protein 1B, and binds tubulin. The STAU gene product has been shown to be present in the cytoplasm in association with the rough endoplasmic reticulum (RER), implicating this protein in the transport of mRNA via the microtubule network to the RER, the site of translation. Five transcript variants resulting from alternative splicing of STAU gene and encoding three isoforms have been described. Three of these variants encode the same isoform, however, differ in their 5'UTR. Application Notes Optimal dilution of the STAU1 antibody should be determined by the researcher. Immunogen Amino acids HGIGKDVESCHDMAALNILKLLSELDQQSTEMPRTGN of human Staufen were used as the immunogen for the STAU1 antibody. Storage After reconstitution, the STAU1 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing. Ordering: Phone:858.663.9055 | Fax:1.267.821.0800 | Email:[email protected] Copyright © NSJ Bioreagents. All rights reserved.

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Lin28b and Mir-142-3P Regulate Neuronal Differentiation by Modulating Staufen1 Expression
Cell Death and Differentiation (2018) 25, 432–443 & 2018 ADMC Associazione Differenziamento e Morte Cellulare All rights reserved 1350-9047/18 www.nature.com/cdd Lin28B and miR-142-3p regulate neuronal differentiation by modulating Staufen1 expression Younseo Oh1,5, Jungyun Park1,5, Jin-Il Kim1, Mi-Yoon Chang2, Sang-Hun Lee3, Youl-Hee Cho*,4 and Jungwook Hwang*,1,4 Staufen1 (STAU1) and Lin28B are RNA-binding proteins that are involved in neuronal differentiation as a function of post- transcriptional regulation. STAU1 triggers post-transcriptional regulation, including mRNA export, mRNA relocation, translation and mRNA decay. Lin28B also has multiple functions in miRNA biogenesis and the regulation of translation. Here, we examined the connection between STAU1 and Lin28B and found that Lin28B regulates the abundance of STAU1 mRNA via miRNA maturation. Decreases in the expression of both STAU1 and Lin28B were observed during neuronal differentiation. Depletion of STAU1 or Lin28B inhibited neuronal differentiation, and overexpression of STAU1 or Lin28B enhanced neuronal differentiation. Interestingly, the stability of STAU1 mRNA was modulated by miR-142-3p, whose maturation was regulated by Lin28B. Thus, miR-142-3p expression increased as Lin28B expression decreased during differentiation, leading to the reduction of STAU1 expression. The transcriptome from Staufen-mediated mRNA decay (SMD) targets during differentiation was analyzed, confirming that STAU1 was a key factor in neuronal differentiation. In support of this finding, regulation of STAU1 expression in mouse neural precursor cells had the same effects on neuronal differentiation as it did in human neuroblastoma cells. These results revealed the collaboration of two RNA-binding proteins, STAU1 and Lin28B, as a regulatory mechanism in neuronal differentiation.
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Staufen2 functions in Staufen1-mediated mRNA decay INAUGURAL ARTICLE by binding to itself and its paralog and promoting UPF1 helicase but not ATPase activity Eonyoung Parka,b, Michael L. Gleghorna,b, and Lynne E. Maquata,b,1 aDepartment of Biochemistry and Biophysics, School of Medicine and Dentistry, and bCenter for RNA Biology, University of Rochester, Rochester, NY 14642 This contribution is part of the special series of Inaugural Articles by members of the National Academy of Sciences elected in 2011. Edited by Michael R. Botchan, University of California, Berkeley, CA, and approved November 16, 2012 (received for review August 3, 2012) Staufen (STAU)1-mediated mRNA decay (SMD) is a posttranscrip- harbor a STAU1-binding site (SBS) downstream of their normal tional regulatory mechanism in mammals that degrades mRNAs termination codon in a pathway called STAU1-mediated mRNA harboring a STAU1-binding site (SBS) in their 3′-untranslated regions decay or SMD (13, 14), and work published by others indicates (3′ UTRs). We show that SMD involves not only STAU1 but also its that SMD does not involve STAU2 (3, 15). paralog STAU2. STAU2, like STAU1, is a double-stranded RNA-binding According to our current model for SMD, when translation protein that interacts directly with the ATP-dependent RNA helicase terminates upstream of an SBS, recruitment of the nonsense-me- diated mRNA decay (NMD) factor UPF1 to SBS-bound STAU1 up-frameshift 1 (UPF1) to reduce the half-life of SMD targets that form ﬂ an SBS by either intramolecular or intermolecular base-pairing. Com- triggers mRNA decay. SMD in uences a number of cellular pro- pared with STAU1, STAU2 binds ∼10-foldmoreUPF1and∼two- to cesses, including the differentiation of mouse C2C12 myoblasts to myotubes (16), the motility of human HaCaT keratinocytes (17), ﬁvefold more of those SBS-containing mRNAs that were tested, and it and the differentiation of mouse 3T3-L1 preadipocytes to adipo- comparably promotes UPF1 helicase activity, which is critical for SMD.
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Staufen 1 Amplifies Pro-Apoptotic Activation of the Unfolded Protein
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Staufen 1 Does Not Play a Role in NPC Asymmetric Divisions but Regulates Cellular Positioning During Corticogenesis
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Non-Canonical Immune Response to the Inhibition of DNA Methylation Via Stabilization Of
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PRODUCT SPECIFICATION Product Datasheet
Product Datasheet QPrEST PRODUCT SPECIFICATION Product Name QPrEST STAU1 Mass Spectrometry Protein Standard Product Number QPrEST22312 Protein Name Double-stranded RNA-binding protein Staufen homolog 1 Uniprot ID O95793 Gene STAU1 Product Description Stable isotope-labeled standard for absolute protein quantification of Double-stranded RNA-binding protein Staufen homolog 1. Lys (13C and 15N) and Arg (13C and 15N) metabolically labeled recombinant human protein fragment. Application Absolute protein quantification using mass spectrometry Sequence (excluding TRPSEQLDYLSRVQGFQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGK fusion tag) DVESCHDMAALNILKLLSELDQQSTEMPRTGNGPMSVCG Theoretical MW 27698 Da including N-terminal His6ABP fusion tag Fusion Tag A purification and quantification tag (QTag) consisting of a hexahistidine sequence followed by an Albumin Binding Protein (ABP) domain derived from Streptococcal Protein G. Expression Host Escherichia coli LysA ArgA BL21(DE3) Purification IMAC purification Purity >90% as determined by Bioanalyzer Protein 230 Purity Assay Isotopic Incorporation >99% Concentration >5 μM after reconstitution in 100 μl H20 Concentration Concentration determined by LC-MS/MS using a highly pure amino acid analyzed internal Determination reference (QTag), CV ≤10%. Amount >0.5 nmol per vial, two vials supplied. Formulation Lyophilized in 100 mM Tris-HCl 5% Trehalose, pH 8.0 Instructions for Spin vial before opening. Add 100 μL ultrapure H2O to the vial. Vortex thoroughly and spin Reconstitution down. For further dilution, see Application Protocol. Shipping Shipped at ambient temperature Storage Lyophilized product shall be stored at -20°C. See COA for expiry date. Reconstituted product can be stored at -20°C for up to 4 weeks. Avoid repeated freeze-thaw cycles. Notes For research use only Product of Sweden. For research use only.
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Staufen1 Inhibits Myod Translation to Actively Maintain Muscle Stem Cell Quiescence
Staufen1 inhibits MyoD translation to actively maintain muscle stem cell quiescence Antoine de Morréea,b,1, Cindy T. J. van Velthovena,b,1, Qiang Gana,b, Jayesh S. Salvia,b, Julian D. D. Kleina,b, Igor Akimenkoa,b, Marco Quartaa,b,c, Stefano Biressia,b,2, and Thomas A. Randoa,b,c,3 aDepartment of Neurology and Neurological Sciences, Stanford University School of Medicine, Stanford, CA 94305; bPaul F. Glenn Center for the Biology of Aging, Stanford University School of Medicine, Stanford, CA 94305; and cCenter for Tissue Regeneration, Repair and Restoration, Veterans Affairs Palo Alto Health Care System, Palo Alto, CA 90304 Edited by Eric N. Olson, University of Texas Southwestern Medical Center, Dallas, TX, and approved September 8, 2017 (received for review May 26, 2017) Tissue regeneration depends on the timely activation of adult stem appearance of MyoD protein has been functionally linked with cells. In skeletal muscle, the adult stem cells maintain a quiescent state MuSC activation and is controlled at the level of transcription and and proliferate upon injury. We show that muscle stem cells (MuSCs) RNA degradation (17, 18). In this paper, we demonstrate that, use direct translational repression to maintain the quiescent state. contrary to prevailing models, quiescent MuSCs express MyoD High-resolution single-molecule and single-cell analyses demonstrate transcript in vivo and actively block MyoD translation. When these that quiescent MuSCs express high levels of Myogenic Differentiation cells activate, they increase protein translation by relieving this 1 (MyoD) transcript in vivo, whereas MyoD protein is absent. RNA translational block. Therefore, MuSCs exist poised for activation pulldowns and costainings show that MyoD mRNA interacts with by the regulation of translation of transcripts present in the qui- Staufen1, a potent regulator of mRNA localization, translation, and escent state.
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