36-2979: Anti-ATRX / RAD54 (Alpha Thalassemia Mental Retardation) Monoclonal Antibody(Clone: 23C)

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36-2979: Anti-ATRX / RAD54 (Alpha Thalassemia Mental Retardation) Monoclonal Antibody(Clone: 23C)

9853 Pacific Heights Blvd. Suite D. San Diego, CA 92121, USA Tel: 858-263-4982 Email: [email protected] 36-2979: Anti-ATRX / RAD54 (Alpha Thalassemia Mental Retardation) Monoclonal Antibody(Clone: 23c) Clonality : Monoclonal Clone Name : 23c Application : ELISA Reactivity : Human Gene : ATRX Gene ID : 546 Uniprot ID : P46100 Alpha thalassemia/mental retardation syndrome X linked homolog; ATP-dependent helicase ATRX; ATR2; ATRX; DNA-dependent ATPase and helicase; MRXHF1; RAD54; RAD54L; SFM1; Alternative Name : SHS; Transcriptional regulator ATRX; X-linked helicase II; X-linked nuclear protein; XH2; XNP; Znf-HX Isotype : Mouse IgG1, kappa Immunogen Information : Recombinant human ATRX protein Description ATRX is a member of the Snf2 family of helicase/ATPases, which contribute to the remodeling of the nucelosome structure in an ATP-dependent manner, and facilitate the initiation of transcription and replication. Structurally, ATRX contains a PHD zinc finger motif. ATRX is regulated throµghout the cell cycle where it is differentially distributed within the nucleus. During interphase, ATRX predominately associates with the nuclear matrix, while during mitosis, ATRX localizes with condensed chromatin. At the onset of M phase, phosphorylation rapidly induces this redistribution of ATRX to the short arms of human acrocentric chromosomes, where it then specifically complexes with heterochromatin protein 1 thalassemia or ATRX syndrome Product Info Amount : 20 µg / 100 µg 200 µg/ml of Ab Purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with Content : 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml. Antibody with azide - store at 2 to 8°C. Antibody without azide - store at -20 to -80°C. Antibody is Storage condition : stable for 24 months. Non-hazardous. Application Note ELISA (Use Ab at 2-4Âµg/ml for coating) (Order Ab without BSA); Optimal dilution for a specific application should be determined. Fig. 1: SDS-PAGE Analysis Purified ATRX Mouse Monoclonal Antibody (23c). Confirmation of Integrity and Purity of Antibody. For Research Use Only. Not for use in diagnostic/therapeutics procedures..

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ATRX Protects Cells Against Replication-Induced Genomic Instability
ATRX Protects Cells Against Replication-Induced Genomic Instability Danton Ivanochko M.Sc. Thesis This thesis is submitted to the Faculty of Graduate and Postdoctoral Studies in partial fulfillment of the requirements for the degree of Master of Science in Biochemistry with a specialization in Human and Molecular Genetics Department of Biochemistry, Microbiology, and Immunology Faculty of Medicine University of Ottawa, Ontario, Ontario, Canada © Danton Ivanochko, Ottawa, Canada, 2016 Dedicated to my parents. ii Abstract Expansive proliferation of neural progenitor cells (NPCs) is a prerequisite to the temporal waves of neuronal differentiation that generate the six-layered cerebral cortex. NPC expansion places a heavy burden on proteins that regulate chromatin packaging and genome integrity, which is further reflected by the growing number of developmental disorders caused by mutations in chromatin regulators. Accordingly, mutations in ATRX, a chromatin remodelling protein required for heterochromatin maintenance at telomeres and simple repeats, cause the ATR-X syndrome. Here, we demonstrate that proliferating ATRX-null cells accumulate DNA damage, while also exhibiting sensitivity to hydroxyurea-induced replication fork stalling. Specifically, PARP1 hyperactivation and replication-dependent double strand DNA breakage indicated replication fork protection defects, while DNA fiber assays confirmed that ATRX was required to protect replication forks from degradation. Interestingly, inhibition of the exonuclease MRE11 by the small molecule mirin could prevent degradation. Thus, ATRX is required to limit replication stress during NPC expansion. iii Acknowledgements First and foremost, I would like to thank my supervisor, Dr. David Picketts, for his guidance and support during my undergraduate and graduate studies. Thanks to the members of my thesis advisory committee, Dr.
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