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Datasheet Version: 1.0.0 Revision date: 01 Nov 2020 Human Bromodomain adjacent to zinc finger domain protein 1A (BAZ1A) ELISA Kit Catalogue No.:abx503566 For the in vitro quantitative measurement of Human Bromodomain adjacent to zinc finger domain protein 1A (BAZ1A) concentrations in tissue homogenates, cell lysates and other biological fluids. Target: Bromodomain adjacent to zinc finger domain protein 1A (BAZ1A) Reactivity: Human Tested Applications: ELISA Recommended dilutions: Optimal dilutions/concentrations should be determined by the end user. Storage: Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. Validity: The validity for this kit is 6 months. Stability: The stability of the kit is determined by the rate of activity loss. The loss rate is less than 5% within the expiration date under appropriate storage conditions. To minimize performance fluctuations, operation procedures and lab conditions should be strictly controlled. It is also strongly suggested that the whole assay is performed by the same user throughout. UniProt Primary AC:ForQ9NRL2 (UniProtReference, ExPASy) Only Gene Symbol: BAZ1A KEGG: hsa:11177 Test Range: 0.156 ng/ml - 10 ng/ml Standard Form: Lyophilized v1.0.0 Abbexa Ltd, Cambridge, UK · Phone: +44 1223 755950 · Fax: +44 1223 755951 1 Abbexa LLC, Houston, TX, USA · Phone: +1 832 327 7413 www.abbexa.com · Email: [email protected] Datasheet Version: 1.0.0 Revision date: 01 Nov 2020 ELISA Detection: Colorimetric ELISA Data: Quantitative Sample Type: Tissue homogenates, cell lysates and other biological fluids. Note: This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. For Reference Only v1.0.0 Abbexa Ltd, Cambridge, UK · Phone: +44 1223 755950 · Fax: +44 1223 755951 2 Abbexa LLC, Houston, TX, USA · Phone: +1 832 327 7413 www.abbexa.com · Email: [email protected].

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Functional Roles of Bromodomain Proteins in Cancer
cancers Review Functional Roles of Bromodomain Proteins in Cancer Samuel P. Boyson 1,2, Cong Gao 3, Kathleen Quinn 2,3, Joseph Boyd 3, Hana Paculova 3 , Seth Frietze 3,4,* and Karen C. Glass 1,2,4,* 1 Department of Pharmaceutical Sciences, Albany College of Pharmacy and Health Sciences, Colchester, VT 05446, USA; [email protected] 2 Department of Pharmacology, Larner College of Medicine, University of Vermont, Burlington, VT 05405, USA; [email protected] 3 Department of Biomedical and Health Sciences, University of Vermont, Burlington, VT 05405, USA; [email protected] (C.G.); [email protected] (J.B.); [email protected] (H.P.) 4 University of Vermont Cancer Center, Burlington, VT 05405, USA * Correspondence: [email protected] (S.F.); [email protected] (K.C.G.) Simple Summary: This review provides an in depth analysis of the role of bromodomain-containing proteins in cancer development. As readers of acetylated lysine on nucleosomal histones, bromod- omain proteins are poised to activate gene expression, and often promote cancer progression. We examined changes in gene expression patterns that are observed in bromodomain-containing proteins and associated with speciﬁc cancer types. We also mapped the protein–protein interaction network for the human bromodomain-containing proteins, discuss the cellular roles of these epigenetic regu- lators as part of nine different functional groups, and identify bromodomain-speciﬁc mechanisms in cancer development. Lastly, we summarize emerging strategies to target bromodomain proteins in cancer therapy, including those that may be essential for overcoming resistance. Overall, this review provides a timely discussion of the different mechanisms of bromodomain-containing pro- Citation: Boyson, S.P.; Gao, C.; teins in cancer, and an updated assessment of their utility as a therapeutic target for a variety of Quinn, K.; Boyd, J.; Paculova, H.; cancer subtypes.
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Loss of ISWI Atpase SMARCA5 (SNF2H) in Acute Myeloid Leukemia Cells Inhibits Proliferation and Chromatid Cohesion
International Journal of Molecular Sciences Article Loss of ISWI ATPase SMARCA5 (SNF2H) in Acute Myeloid Leukemia Cells Inhibits Proliferation and Chromatid Cohesion 1, 1, 1 2,3,4 1 Tomas Zikmund y , Helena Paszekova y , Juraj Kokavec , Paul Kerbs , Shefali Thakur , Tereza Turkova 1, Petra Tauchmanova 1, Philipp A. Greif 2,3,4 and Tomas Stopka 1,* 1 Biocev, 1st Medical Faculty, Charles University, 25250 Vestec, Czech Republic; [email protected] (T.Z.); [email protected] (H.P.); [email protected] (J.K.); [email protected] (S.T.); [email protected] (T.T.); [email protected] (P.T.) 2 Department of Medicine III, University Hospital, LMU Munich, D-80539 Munich, Germany; [email protected] (P.K.); [email protected] (P.A.G.) 3 German Cancer Consortium (DKTK), partner site Munich, D-80336 Munich, Germany 4 German Cancer Research Center (DKFZ), D-69120 Heidelberg, Germany * Correspondence: [email protected]; Tel.: +420-32587-3001 These authors contributed equally. y Received: 26 February 2020; Accepted: 16 March 2020; Published: 18 March 2020 Abstract: ISWI chromatin remodeling ATPase SMARCA5 (SNF2H) is a well-known factor for its role in regulation of DNA access via nucleosome sliding and assembly. SMARCA5 transcriptionally inhibits the myeloid master regulator PU.1. Upregulation of SMARCA5 was previously observed in CD34+ hematopoietic progenitors of acute myeloid leukemia (AML) patients. Since high levels of SMARCA5 are necessary for intensive cell proliferation and cell cycle progression of developing hematopoietic stem and progenitor cells in mice, we reasoned that removal of SMARCA5 enzymatic activity could aﬀect the cycling or undiﬀerentiated state of leukemic progenitor-like clones.
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The Function and Evolution of C2H2 Zinc Finger Proteins and Transposons
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Copyright © 2012 by James A. Dowdle All rights reserved DEDICATION This work is dedicated to my loving parents and grandparents who have never stood in the way of letting me be me and for selflessly ensuring and continuing to ensure that I have every opportunity to succeed. Also, in loving memory of my Grams who made the best damn Michigan the world has ever known. A fellow scientist once reminded me that: “Science is boring, boring, boring, boring (breath), boring, boring, exciting! and that is why we keep doing what we do.” iii ABSTRACT Acf1 was isolated almost 15 years ago from Drosophila embryo extracts as a subunit of several complexes that possess chromatin assembly activity. Acf1 binds to the ATPase Iswi (SNF2H in mammals) to form the ACF and CHRAC chromatin remodeling complexes, which can slide nucleosomes and assemble arrays of regularly spaced nucleosomes in vitro. Evidence from Drosophila and from human and mouse cell culture studies implicates Acf1 in a wide range of cellular processes including transcriptional repression, heterochromatin formation and replication, and DNA damage checkpoints and repair. However, despite these studies, little is known about the in vivo function of Acf1 in mammals. This thesis is focused on elucidating the role of mouse Baz1a, which is the closest mammalian homolog of Acf1 from Drosophila. The study began by characterizing the expression of Baz1a, which revealed high expression in the testis, and continued with analysis of unique splice variants and the subcellular localization of the protein product in this organ. Next, Baz1a-deficient mice were generated to investigate the role of this factor during development.
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