Rabbit Anti-DAZAP1/FITC Conjugated Antibody-SL14200R-FITC

Total Page:16

File Type:pdf, Size:1020Kb

Rabbit Anti-DAZAP1/FITC Conjugated Antibody-SL14200R-FITC SunLong Biotech Co.,LTD Tel: 0086-571- 56623320 Fax:0086-571- 56623318 E-mail:[email protected] www.sunlongbiotech.com Rabbit Anti-DAZAP1/FITC Conjugated antibody SL14200R-FITC Product Name: Anti-DAZAP1/FITC Chinese Name: FITC标记的无精症缺失相关蛋白1抗体 DAZ associated protein 1; DAZ-associated protein 1; Dazap1; DAZP1_HUMAN; Alias: Deleted in azoospermia associated protein 1; Deleted in azoospermia-associated protein 1. Organism Species: Rabbit Clonality: Polyclonal React Species: Human,Mouse,Rat,Chicken,Dog,Pig,Cow,Horse,Sheep, ICC=1:50-200IF=1:50-200 Applications: not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. Molecular weight: 43kDa Form: Lyophilized or Liquid Concentration: 1mg/ml immunogen: KLH conjugated synthetic peptide derived from human DAZAP1 Lsotype: IgG Purification: affinity purified by Protein A Storage Buffer: 0.01Mwww.sunlongbiotech.com TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year Storage: when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. background: In mammals, the Y chromosome directs the development of the testes and plays an important role in spermatogenesis. A high percentage of infertile men have deletions that map to regions of the Y chromosome. The DAZ (deleted in azoospermia) gene Product Detail: cluster maps to the AZFc region of the Y chromosome and is deleted in many azoospermic and severely oligospermic men. It is thought that the DAZ gene cluster arose from the transposition, amplification, and pruning of the ancestral autosomal gene DAZL also involved in germ cell development and gametogenesis. This gene encodes a RNA-binding protein with two RNP motifs that was originally identified by its interaction with the infertility factors DAZ and DAZL. Two isoforms are encoded by transcript variants of this gene. [provided by RefSeq, Jul 2008] Function: RNA-binding protein, which may be required during spermatogenesis. Subcellular Location: Cytoplasm. Nucleus. Predominantly cytoplasmic (By similarity). Nuclear at some stages of spermatozoides development. In midpachytene spermatocytes, it is localized in both the cytoplasm and the nuclei and is clearly excluded from the sex vesicles. In round spermatids, it localizes mainly in the nuclei, whereas in elongated spermatids, it localizes to the cytoplasm. Tissue Specificity: Mainly expressed in testis. Expressed to a lower level in thymus. Weakly or not expressed in heart, liver, brain, placenta, lung, skeletal muscle, kidney and pancreas. Post-translational modifications: Phosphorylated upon DNA damage, probably by ATM or ATR. Similarity: Contains 2 RRM (RNA recognition motif) domains. Database links: Entrez Gene: 26528 Human Entrez Gene: 427266 Chicken Entrez Gene: 614783 Cow Entrez Gene: 100683271 Dog Entrezwww.sunlongbiotech.com Gene: 70248 Mouse Entrez Gene: 100433715 Orangutan Entrez Gene: 100625005 Pig Entrez Gene: 362836 Rat Entrez Gene: 707132 Rhesus monkey Entrez Gene: 398218 Xenopus laevis Entrez Gene: 448406 Xenopus tropicalis Omim: 607430 Human SwissProt: Q96EP5 Human SwissProt: Q9JII5 Mouse SwissProt: Q98SJ2 Xenopus laevis Unigene: 222510 Human Unigene: 148693 Mouse Unigene: 16769 Rat Unigene: 1666 Xenopus laevis Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. www.sunlongbiotech.com.
Recommended publications
  • Rashid Thesis 2015
    Protein Profile and Directed Gene Expression of Developing C2C12 cells By Susan Rashid Submitted in Partial Fulfillment of the Requirements For the Degree of Master of Science In the Biological Sciences Program YOUNGSTOWN STATE UNIVERSITY August 3, 2015 Protein Profile and Directed Gene Expression of Developing C2C12 cells Susan Rashid I hereby release this thesis to the public. I understand that this will be made available from the OhioLINK ETD Center and the Maag Library Circulation Desk for public access. I also authorize the University or other individuals to make copies of this thesis as needed for scholarly research. Signature: ___________________________________________________ Susan Rashid, Student Date Approvals: ___________________________________________________ Dr. Gary Walker, Thesis Advisor 'ate ___________________________________________________ Dr. Jonathan Caguiat, Committee Member Date ___________________________________________________ Dr. David Asch, Committee Member Date ___________________________________________________ Dr. Sal Sanders, Associate Dean, Graduate Studies Date ABSTRACT Myogenesis is a tightly regulated process resulting in unique structures called myotubes or myofibers, which compose skeletal muscle. Myotubes are multi-nucleated fibers containing a functional unit composed of cytoskeletal proteins called the sarcomere. The specific arrangement of these proteins in the sarcomere works to contract and relax muscles. During embryonic and post-embryonic development, fluctuations in expression of growth factors throughout the program account for the dramatic structural changes from cell to mature muscle fiber. In vivo, these growth factors are strictly spatiotemporally regulated according to a ‘myogenic program.’ In order to assess the dynamics of protein expression throughout this program, we conducted a time course study using the mouse myoblast cell line C2C12, in which cells were allowed to differentiate and insoluble protein fractions were collected at seven time points.
    [Show full text]
  • Molecularly Imprinted Polymers for the Analysis of Protein Phosphorylation and the Role of Htra2/Omi Protein in Parkinson's Disease
    Molecularly Imprinted Polymers for the Analysis of Protein Phosphorylation and the Role of HtrA2/Omi Protein in Parkinson's Disease by Jing Chen Dissertation Submitted to the Faculty of Chemistry and Biochemistry In Candidacy for the Degree of Doctor Rerum Naturalium (Dr. rer. nat) Accomplished at Medizinisches Proteom-Center Ruhr-Universität Bochum, Germany 03. 2015, Bochum Statement in Lieu of Oath I hereby declare that I have accomplished the thesis independently and did not submit to any other faculty or refer to more than the publications listed in the references. The digital figures contain only original data and no modification was added. There are altogether 5 identical copies of my dissertation. __________________________ Jing Chen I Referee: Prof. Dr. Katrin Marcus Co-referee: Dr. Dirk Wolters II Acknowledgement I would like to express my deep and sincere gratitude to Prof. Dr. Katrin Marcus, director of the Medizinische Proteom-Center, for her friendly invitation to the working group, for the great opportunity working in the interesting research field, for her dedication in supervising of my project execution and her unconditional help at the end of my Ph.D. I am very grateful to Dr. Dirk Wolters for his kind acceptance of attending and co- judging my dissertation. I owe my sincere gratitude to Dr. Stefan Helling, for his outstanding mentoring to this work. His valuable advice is deciding. Hadn’t for his endeavor in discussing and clearing my confusion at all times, I wouldn’t have managed to accomplish the work. I know Prof. Dr. Börje Sellergren, my collaboration partner at biomedical science in Malmö University, Sweden the longest.
    [Show full text]
  • Genetic Dissection of the AZF Regions of the Human Y Chromosome: Thriller Or Filler for Male (In)Fertility?
    Hindawi Publishing Corporation Journal of Biomedicine and Biotechnology Volume 2010, Article ID 936569, 18 pages doi:10.1155/2010/936569 Review Article Genetic Dissection of the AZF Regions of the Human Y Chromosome: Thriller or Filler for Male (In)fertility? Paulo Navarro-Costa,1, 2, 3 Carlos E. Plancha,2 and Joao˜ Gonc¸alves1 1 Departamento de Gen´etica, Instituto Nacional de Saude´ Dr. Ricardo Jorge, 1649-016 Lisboa, Portugal 2 Faculdade de Medicina de Lisboa, Instituto de Histologia e Biologia do Desenvolvimento, 1649-028 Lisboa, Portugal 3 Faculdade de Medicina de Lisboa, Instituto de Medicina Molecular, 1649-028 Lisboa, Portugal Correspondence should be addressed to Paulo Navarro-Costa, [email protected] Received 17 December 2009; Accepted 23 April 2010 Academic Editor: Brynn Levy Copyright © 2010 Paulo Navarro-Costa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The azoospermia factor (AZF) regions consist of three genetic domains in the long arm of the human Y chromosome referred to as AZFa, AZFb and AZFc. These are of importance for male fertility since they are home to genes required for spermatogenesis. In this paper a comprehensive analysis of AZF structure and gene content will be undertaken. Particular care will be given to the molecular mechanisms underlying the spermatogenic impairment phenotypes associated to AZF deletions. Analysis of the 14 different AZF genes or gene families argues for the existence of functional asymmetries between the determinants; while some are prominent players in spermatogenesis, others seem to modulate more subtly the program.
    [Show full text]
  • Table S3a Table
    Table S3a C2 KEGG Geneset Genesets enriched and upregulated in responders (FDR <0.25) Genesets enriched and upregulated in non-responders (FDR <0.25) HSA04610_COMPLEMENT_AND_COAGULATION_CASCADES HSA00970_AMINOACYL_TRNA_BIOSYNTHESIS HSA04640_HEMATOPOIETIC_CELL_LINEAGE HSA05050_DENTATORUBROPALLIDOLUYSIAN_ATROPHY HSA04060_CYTOKINE_CYTOKINE_RECEPTOR_INTERACTION HSA04514_CELL_ADHESION_MOLECULES HSA04650_NATURAL_KILLER_CELL_MEDIATED_CYTOTOXICITY HSA04630_JAK_STAT_SIGNALING_PATHWAY HSA03320_PPAR_SIGNALING_PATHWAY HSA04080_NEUROACTIVE_LIGAND_RECEPTOR_INTERACTION HSA00980_METABOLISM_OF_XENOBIOTICS_BY_CYTOCHROME_P450 HSA00071_FATTY_ACID_METABOLISM HSA04660_T_CELL_RECEPTOR_SIGNALING_PATHWAY HSA04612_ANTIGEN_PROCESSING_AND_PRESENTATION HSA04662_B_CELL_RECEPTOR_SIGNALING_PATHWAY HSA04920_ADIPOCYTOKINE_SIGNALING_PATHWAY HSA00120_BILE_ACID_BIOSYNTHESIS HSA04670_LEUKOCYTE_TRANSENDOTHELIAL_MIGRATION HSA00641_3_CHLOROACRYLIC_ACID_DEGRADATION HSA04020_CALCIUM_SIGNALING_PATHWAY HSA04940_TYPE_I_DIABETES_MELLITUS HSA04512_ECM_RECEPTOR_INTERACTION HSA00010_GLYCOLYSIS_AND_GLUCONEOGENESIS HSA02010_ABC_TRANSPORTERS_GENERAL HSA04664_FC_EPSILON_RI_SIGNALING_PATHWAY HSA04710_CIRCADIAN_RHYTHM HSA04510_FOCAL_ADHESION HSA04810_REGULATION_OF_ACTIN_CYTOSKELETON HSA00410_BETA_ALANINE_METABOLISM HSA01040_POLYUNSATURATED_FATTY_ACID_BIOSYNTHESIS HSA00532_CHONDROITIN_SULFATE_BIOSYNTHESIS HSA04620_TOLL_LIKE_RECEPTOR_SIGNALING_PATHWAY HSA04010_MAPK_SIGNALING_PATHWAY HSA00561_GLYCEROLIPID_METABOLISM HSA00053_ASCORBATE_AND_ALDARATE_METABOLISM HSA00590_ARACHIDONIC_ACID_METABOLISM
    [Show full text]
  • Accurate Prediction of Kinase-Substrate Networks Using
    bioRxiv preprint doi: https://doi.org/10.1101/865055; this version posted December 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 4.0 International license. Accurate Prediction of Kinase-Substrate Networks Using Knowledge Graphs V´ıtNov´aˇcek1∗+, Gavin McGauran3, David Matallanas3, Adri´anVallejo Blanco3,4, Piero Conca2, Emir Mu~noz1,2, Luca Costabello2, Kamalesh Kanakaraj1, Zeeshan Nawaz1, Sameh K. Mohamed1, Pierre-Yves Vandenbussche2, Colm Ryan3, Walter Kolch3,5,6, Dirk Fey3,6∗ 1Data Science Institute, National University of Ireland Galway, Ireland 2Fujitsu Ireland Ltd., Co. Dublin, Ireland 3Systems Biology Ireland, University College Dublin, Belfield, Dublin 4, Ireland 4Department of Oncology, Universidad de Navarra, Pamplona, Spain 5Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland 6School of Medicine, University College Dublin, Belfield, Dublin 4, Ireland ∗ Corresponding authors ([email protected], [email protected]). + Lead author. 1 bioRxiv preprint doi: https://doi.org/10.1101/865055; this version posted December 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 4.0 International license. Abstract Phosphorylation of specific substrates by protein kinases is a key control mechanism for vital cell-fate decisions and other cellular pro- cesses. However, discovering specific kinase-substrate relationships is time-consuming and often rather serendipitous.
    [Show full text]
  • Hormone and Inhibitor Treatment T47DM Cells Were Used for All Experiments Unless Otherwise Stated
    Extended Data Extended Materials Methods Cell culture; hormone and inhibitor treatment T47DM cells were used for all experiments unless otherwise stated. For hormone induction experiments, cells were grown in RPMI medium without Phenol Red, supplemented with 10% dextran-coated charcoal-treated FBS (DCC/FBS) after 24 h in serum-free conditions; cells were incubated with R5020 (10 nM) or vehicle (ethanol) as described (Vicent et al. 2011). For hormone induction experiments in MCF7 cells a similar procedure was performed; cells were grown in DMEM medium without Phenol Red, supplemented with 10% dextran-coated charcoal-treated FBS (DCC/FBS) after 24 h in serum-free conditions; cells were incubated with Estradiol (10 nM) or vehicle (ethanol). PARG and PARP inhibition were carried out via incubating cells with 5uM TA (tannic acid) or 10uM 3AB (3-amino-benzamide) respectively 1 hour prior to hormone treatment. All transfections were performed using Lipofectamine2000 (Invitrogen) according to manufacturers instructions. PAR-capture ELISA Hormone and or inhibitor treatments were carried out as described, and sample preparation was carried out as follows: At the required time point, cells were washed twice with ice-cold PBS and scraped in lysis buffer (0.4 M NaCl, 1% Triton X-100) plus protease inhibitors. Cell suspensions were then incubated for 30 min on ice with periodic vortexing. The disrupted cell suspension was centrifuged at 10,000g for 10 min at 4°C, and the supernatant was recovered, snap-frozen, and stored at 80°C until required. Ninety-six-well black-walled plates were incubated with 2 ng/mL anti-PAR monoclonal antibody (Trevigen) in 50 mM sodium carbonate (pH 7.6) overnight at 4°C.
    [Show full text]
  • A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression
    Supplementary Materials A Meta-Analysis of the Effects of High-LET Ionizing Radiations in Human Gene Expression Table S1. Statistically significant DEGs (Adj. p-value < 0.01) derived from meta-analysis for samples irradiated with high doses of HZE particles, collected 6-24 h post-IR not common with any other meta- analysis group. This meta-analysis group consists of 3 DEG lists obtained from DGEA, using a total of 11 control and 11 irradiated samples [Data Series: E-MTAB-5761 and E-MTAB-5754]. Ensembl ID Gene Symbol Gene Description Up-Regulated Genes ↑ (2425) ENSG00000000938 FGR FGR proto-oncogene, Src family tyrosine kinase ENSG00000001036 FUCA2 alpha-L-fucosidase 2 ENSG00000001084 GCLC glutamate-cysteine ligase catalytic subunit ENSG00000001631 KRIT1 KRIT1 ankyrin repeat containing ENSG00000002079 MYH16 myosin heavy chain 16 pseudogene ENSG00000002587 HS3ST1 heparan sulfate-glucosamine 3-sulfotransferase 1 ENSG00000003056 M6PR mannose-6-phosphate receptor, cation dependent ENSG00000004059 ARF5 ADP ribosylation factor 5 ENSG00000004777 ARHGAP33 Rho GTPase activating protein 33 ENSG00000004799 PDK4 pyruvate dehydrogenase kinase 4 ENSG00000004848 ARX aristaless related homeobox ENSG00000005022 SLC25A5 solute carrier family 25 member 5 ENSG00000005108 THSD7A thrombospondin type 1 domain containing 7A ENSG00000005194 CIAPIN1 cytokine induced apoptosis inhibitor 1 ENSG00000005381 MPO myeloperoxidase ENSG00000005486 RHBDD2 rhomboid domain containing 2 ENSG00000005884 ITGA3 integrin subunit alpha 3 ENSG00000006016 CRLF1 cytokine receptor like
    [Show full text]
  • Genetic Dissection of the AZF Regions of the Human Y Chromosome: Thriller Or Filler for Male (In)Fertility?
    Hindawi Publishing Corporation Journal of Biomedicine and Biotechnology Volume 2010, Article ID 936569, 18 pages doi:10.1155/2010/936569 Review Article Genetic Dissection of the AZF Regions of the Human Y Chromosome: Thriller or Filler for Male (In)fertility? Paulo Navarro-Costa,1, 2, 3 Carlos E. Plancha,2 and Joao˜ Gonc¸alves1 1 Departamento de Gen´etica, Instituto Nacional de Saude´ Dr. Ricardo Jorge, 1649-016 Lisboa, Portugal 2 Faculdade de Medicina de Lisboa, Instituto de Histologia e Biologia do Desenvolvimento, 1649-028 Lisboa, Portugal 3 Faculdade de Medicina de Lisboa, Instituto de Medicina Molecular, 1649-028 Lisboa, Portugal Correspondence should be addressed to Paulo Navarro-Costa, [email protected] Received 17 December 2009; Accepted 23 April 2010 Academic Editor: Brynn Levy Copyright © 2010 Paulo Navarro-Costa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The azoospermia factor (AZF) regions consist of three genetic domains in the long arm of the human Y chromosome referred to as AZFa, AZFb and AZFc. These are of importance for male fertility since they are home to genes required for spermatogenesis. In this paper a comprehensive analysis of AZF structure and gene content will be undertaken. Particular care will be given to the molecular mechanisms underlying the spermatogenic impairment phenotypes associated to AZF deletions. Analysis of the 14 different AZF genes or gene families argues for the existence of functional asymmetries between the determinants; while some are prominent players in spermatogenesis, others seem to modulate more subtly the program.
    [Show full text]
  • Factors Regulating the Function and Assembly of the Sarcoglycan Complex in Brain
    Factors regulating the function and assembly of the sarcoglycan complex in brain A thesis submitted for the Degree of Doctor of Philosophy at Cardiff University School of Medicine Francesca Carlisle 2016 Supervised by Professor Derek Blake and Professor Anthony Isles Thesis summary Myoclonus dystonia (MD) is a neurogenic movement disorder that can be caused by mutations in the SGCE gene encoding ε-sarcoglycan. ε-sarcoglycan belongs to the sarcoglycan family of cell surface-localised, single-pass transmembrane proteins originally identified in muscle where they form a heterotetrameric subcomplex of the dystrophin- associated glycoprotein complex (DGC). Mutations in the SGCA, SGCB, SGCG and SGCD genes encoding α-, β-, γ- and δ-sarcoglycan cause limb-girdle muscular dystrophy (LGMD). There is no phenotypic overlap between MD and LGMD. LGMD-associated sarcoglycan mutations impair trafficking of the entire sarcoglycan complex to the cell surface and destabilise the DGC in muscle, while MD-associated mutations typically result in loss of ε- sarcoglycan from the cell surface. This suggests cell surface ε-sarcoglycan but not other sarcoglycans is required for normal brain function. To gain insight into ε-sarcoglycan’s function(s) in the brain, immunoaffinity purification was used to identify ε-sarcoglycan- interacting proteins. Ubiquitous and brain-specific ε-sarcoglycan isoforms co-purified with three other sarcoglycans including ζ-sarcoglycan (encoded by SGCZ) from the brain. Incorporation of an LGMD-associated β-sarcoglycan mutant into the brain sarcoglycan complex impaired the formation of the βδ-sarcoglycan core but failed to abrogate the association and trafficking of ε- and ζ-sarcoglycan in heterologous cells. Both ε-sarcoglycan isoforms also co-purified with β-dystroglycan, indicating inclusion in DGC-like complexes.
    [Show full text]
  • Pathogenic Nssnps That Increase the Risks of Cancers Among the Orang
    www.nature.com/scientificreports OPEN Pathogenic nsSNPs that increase the risks of cancers among the Orang Asli and Malays Nurul Ain Khoruddin1,2, Mohd NurFakhruzzaman Noorizhab1,3, Lay Kek Teh1,3, Farida Zuraina Mohd Yusof1,2 & Mohd Zaki Salleh1,3* Single-nucleotide polymorphisms (SNPs) are the most common genetic variations for various complex human diseases, including cancers. Genome-wide association studies (GWAS) have identifed numerous SNPs that increase cancer risks, such as breast cancer, colorectal cancer, and leukemia. These SNPs were cataloged for scientifc use. However, GWAS are often conducted on certain populations in which the Orang Asli and Malays were not included. Therefore, we have developed a bioinformatic pipeline to mine the whole-genome sequence databases of the Orang Asli and Malays to determine the presence of pathogenic SNPs that might increase the risks of cancers among them. Five diferent in silico tools, SIFT, PROVEAN, Poly-Phen-2, Condel, and PANTHER, were used to predict and assess the functional impacts of the SNPs. Out of the 80 cancer-related nsSNPs from the GWAS dataset, 52 nsSNPs were found among the Orang Asli and Malays. They were further analyzed using the bioinformatic pipeline to identify the pathogenic variants. Three nsSNPs; rs1126809 (TYR), rs10936600 (LRRC34), and rs757978 (FARP2), were found as the most damaging cancer pathogenic variants. These mutations alter the protein interface and change the allosteric sites of the respective proteins. As TYR , LRRC34, and FARP2 genes play important roles in numerous cellular processes such as cell proliferation, diferentiation, growth, and cell survival; therefore, any impairment on the protein function could be involved in the development of cancer.
    [Show full text]
  • Ep 2811298 A1
    (19) TZZ __ _T (11) EP 2 811 298 A1 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 10.12.2014 Bulletin 2014/50 G01N 33/53 (2006.01) G01N 33/542 (2006.01) (21) Application number: 13002949.9 (22) Date of filing: 07.06.2013 (84) Designated Contracting States: (72) Inventors: AL AT BE BG CH CY CZ DE DK EE ES FI FR GB • Hall, Jonathan GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO 4143 Dornach (CH) PL PT RO RS SE SI SK SM TR • Pradere, Ugo Designated Extension States: 8046 Zürich (CH) BA ME •Roos,Martina 8050 Zürich (CH) (71) Applicant: ETH Zurich 8092 Zurich (CH) (54) FRET-Method for identifying a biomolecule-modulating compound (57) The present invention relates to a method for the excitation energy spectrum of the fluorophore accep- identifying a compound modulating an interaction be- tor or the energy spectrum absorbed by the dark quench- tween two biomolecules or two domains of one biomol- er overlap at least partially. Preferably, the first and sec- ecule, the first biomolecule or first domain comprising at ond biomolecules are selected from the group consisting least one fluorophore donor and the second biomolecule of polypeptides, sugars, polynucleotides, polyamines or second domain comprising at least one fluorophore and lipids, and more preferably the first biomolecule is acceptor or a dark quencher, wherein the fluorophore selected from the group consisting of polypeptides inter- donor and fluorophore acceptor or the fluorophore donor acting with polynucleotides and the second biomolecule and dark quencher are spectrally paired such that the is selected from the group consisting of polynucleotides, energy spectrum emitted by.the fluorophore donor and preferably microRNAs (miRNA).
    [Show full text]
  • The Analysis of the Mcf7 Cancer Model System And
    THE ANALYSIS OF THE MCF7 CANCER MODEL SYSTEM AND THE EFFECTS OF 5-AZA-2’-DEOXYCYTIDINE TREATMENT ON THE CHROMATIN STATE USING A NOVEL MICROARRAY-BASED TECHNOLOGY FOR HIGH RESOLUTION GLOBAL CHROMATIN STATE MEASUREMENT APPROVED BY SUPERVISORY COMMITTEE Harold Garner, Ph.D. Elliott Ross, Ph.D. Thomas Kodadek, Ph.D. John Minna, M.D. Keith Wharton, M.D., Ph.D. DEDICATION Omnibus qui adiuverunt THE ANALYSIS OF THE MCF7 CANCER MODEL SYSTEM AND THE EFFECTS OF 5-AZA-2’-DEOXYCYTIDINE TREATMENT ON THE CHROMATIN STATE USING A NOVEL MICROARRAY-BASED TECHNOLOGY FOR HIGH RESOLUTION GLOBAL CHROMATIN STATE MEASUREMENT by MICHAEL RYAN WEIL DISSERTATION Presented to the Faculty of the Graduate School of Biomedical Sciences The University of Texas Southwestern Medical Center at Dallas In Partial Fulfillment of the Requirements For the Degree of DOCTOR OF PHILOSOPHY The University of Texas Southwestern Medical Center at Dallas Dallas, Texas March, 2006 Copyright by Michael Ryan Weil All Rights Reserved THE ANALYSIS OF THE MCF7 CANCER MODEL SYSTEM AND THE EFFECTS OF 5-AZA-2’-DEOXYCYTIDINE TREATMENT ON THE CHROMATIN STATE USING A NOVEL MICROARRAY-BASED TECHNOLOGY FOR HIGH RESOLUTION GLOBAL CHROMATIN STATE MEASUREMENT Publication No. MICHAEL RYAN WEIL, B.S. The University of Texas Southwestern Medical Center at Dallas, 2006 Supervising Professor: Harold Ray (Skip) Garner, Ph.D. A microarray method to measure the global chromatin state of the human genome was developed in order to provide a novel view of gene regulation. The 'chromatin array' employs traditional methods of chromatin isolation, microarray technology, and advanced data analysis, and was applied to a cancer model system.
    [Show full text]