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ABI2 (ABI-2, ABI2B, AblBP3, AIP-1, argBPIA, SSH3BP2, ARGBPIA, Abl interactor 2) Catalog number 144114 Supplier United States Biological ABI2 (ABL Interactor 2), is a protein that in humans is encoded by the ABI2 gene. By analysis of a YAC and a BAC, Machado et al. (2000) mapped the ABI2 gene to 2q31-q33. ABI2 possesses a basic N terminus with homology to a homeodomain protein; a central serine-rich region; 3 PEST sequences, which are implicated in susceptibility to protein degradation; several proline-rich stretches; and an acidic C terminus with multiple phosphorylation sites and an SH3 domain. Dai and Pendergast (1995) suggested that the ABI proteins may function to coordinate the cytoplasmic and nuclear functions of the ABL1 tyrosine kinase. UniProt Number Q9NYB9 Gene ID ABI2 Applications Suitable for use in Western Blot. Recommended Dilution Optimal dilutions to be determined by the researcher. Storage and Handling Store at -20˚C for one year. After reconstitution, store at 4˚C for one month. Can also be aliquoted and stored frozen at -20˚C for long term. Avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Immunogen A synthetic peptide corresponding to a sequence at the N-terminal of human ABI2, identical to the related mouse and rat sequences. Formulation Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml. Purity Purified by immunoaffinity chromatography. Specificity Recognizes human,mouse and rat ABI2. No crossreactivity with other proteins. Product Type Pab Source human Isotype IgG Grade Affinity Purified Applications WB Crossreactivity Hu Mo Rt Storage 4°C/-20°C Reference 1. Dai, Z., Pendergast, A. M. Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity. Genes Dev. 9: 2569-2582, 1995. 2. Machado, R. D., Pauciulo, M. W., Fretwell, N., Veal, C., Thomson, J. R., Guell, C. V., Aldred, M., Brannon, C. A., the International PPH Consortium, Trembath, R. C., Nichols, W. C. A physical and transcript map based upon refinement of the critical interval for PPH1, a gene for familial primary pulmonary hypertension. Genomics 68: 220-228, 2000. Powered by TCPDF (www.tcpdf.org).

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Molecular BioSystems Accepted Manuscript This is an Accepted Manuscript, which has been through the Royal Society of Chemistry peer review process and has been accepted for publication. Accepted Manuscripts are published online shortly after acceptance, before technical editing, formatting and proof reading. Using this free service, authors can make their results available to the community, in citable form, before we publish the edited article. We will replace this Accepted Manuscript with the edited and formatted Advance Article as soon as it is available. You can find more information about Accepted Manuscripts in the Information for Authors. Please note that technical editing may introduce minor changes to the text and/or graphics, which may alter content. The journal’s standard Terms & Conditions and the Ethical guidelines still apply. In no event shall the Royal Society of Chemistry be held responsible for any errors or omissions in this Accepted Manuscript or any consequences arising from the use of any information it contains. www.rsc.org/molecularbiosystems Page 1 of 29 Molecular BioSystems Mutated Genes and Driver Pathways Involved in Myelodysplastic Syndromes—A Transcriptome Sequencing Based Approach Liang Liu1*, Hongyan Wang1*, Jianguo Wen2*, Chih-En Tseng2,3*, Youli Zu2, Chung-che Chang4§, Xiaobo Zhou1§ 1 Center for Bioinformatics and Systems Biology, Division of Radiologic Sciences, Wake Forest University Baptist Medical Center, Winston-Salem, NC 27157, USA. 2 Department of Pathology, the Methodist Hospital Research Institute,
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Early Growth Response 1 Regulates Hematopoietic Support and Proliferation in Human Primary Bone Marrow Stromal Cells
Hematopoiesis SUPPLEMENTARY APPENDIX Early growth response 1 regulates hematopoietic support and proliferation in human primary bone marrow stromal cells Hongzhe Li, 1,2 Hooi-Ching Lim, 1,2 Dimitra Zacharaki, 1,2 Xiaojie Xian, 2,3 Keane J.G. Kenswil, 4 Sandro Bräunig, 1,2 Marc H.G.P. Raaijmakers, 4 Niels-Bjarne Woods, 2,3 Jenny Hansson, 1,2 and Stefan Scheding 1,2,5 1Division of Molecular Hematology, Department of Laboratory Medicine, Lund University, Lund, Sweden; 2Lund Stem Cell Center, Depart - ment of Laboratory Medicine, Lund University, Lund, Sweden; 3Division of Molecular Medicine and Gene Therapy, Department of Labora - tory Medicine, Lund University, Lund, Sweden; 4Department of Hematology, Erasmus MC Cancer Institute, Rotterdam, the Netherlands and 5Department of Hematology, Skåne University Hospital Lund, Skåne, Sweden ©2020 Ferrata Storti Foundation. This is an open-access paper. doi:10.3324/haematol. 2019.216648 Received: January 14, 2019. Accepted: July 19, 2019. Pre-published: August 1, 2019. Correspondence: STEFAN SCHEDING - [email protected] Li et al.: Supplemental data 1. Supplemental Materials and Methods BM-MNC isolation Bone marrow mononuclear cells (BM-MNC) from BM aspiration samples were isolated by density gradient centrifugation (LSM 1077 Lymphocyte, PAA, Pasching, Austria) either with or without prior incubation with RosetteSep Human Mesenchymal Stem Cell Enrichment Cocktail (STEMCELL Technologies, Vancouver, Canada) for lineage depletion (CD3, CD14, CD19, CD38, CD66b, glycophorin A). BM-MNCs from fetal long bones and adult hip bones were isolated as reported previously 1 by gently crushing bones (femora, tibiae, fibulae, humeri, radii and ulna) in PBS+0.5% FCS subsequent passing of the cell suspension through a 40-µm filter.
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EAR1 Negatively Regulates ABA Signaling by Enhancing 2C Protein Phosphatase Activity [OPEN]
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Variation in Protein Coding Genes Identifies Information Flow
bioRxiv preprint doi: https://doi.org/10.1101/679456; this version posted June 21, 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. Animal complexity and information flow 1 1 2 3 4 5 Variation in protein coding genes identifies information flow as a contributor to 6 animal complexity 7 8 Jack Dean, Daniela Lopes Cardoso and Colin Sharpe* 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 Institute of Biological and Biomedical Sciences 25 School of Biological Science 26 University of Portsmouth, 27 Portsmouth, UK 28 PO16 7YH 29 30 * Author for correspondence 31 [email protected] 32 33 Orcid numbers: 34 DLC: 0000-0003-2683-1745 35 CS: 0000-0002-5022-0840 36 37 38 39 40 41 42 43 44 45 46 47 48 49 Abstract bioRxiv preprint doi: https://doi.org/10.1101/679456; this version posted June 21, 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. Animal complexity and information flow 2 1 Across the metazoans there is a trend towards greater organismal complexity. How 2 complexity is generated, however, is uncertain. Since C.elegans and humans have 3 approximately the same number of genes, the explanation will depend on how genes are 4 used, rather than their absolute number.
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Tripartite Motif Protein 32 Facilitates Cell Growth and Migration Via Degradation of Abl-Interactor 2
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A Cluster of ABA-Regulated Genes on Arabidopsis Thaliana BAC T07M07 Ming Li Wang,1,2,3 Stephen Belmonte,2 Ulandt Kim,2,4 Maureen Dolan,2,5 John W
Downloaded from genome.cshlp.org on October 5, 2021 - Published by Cold Spring Harbor Laboratory Press Research A Cluster of ABA-Regulated Genes on Arabidopsis thaliana BAC T07M07 Ming Li Wang,1,2,3 Stephen Belmonte,2 Ulandt Kim,2,4 Maureen Dolan,2,5 John W. Morris,2,6 and Howard M. Goodman1,2,7 1Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115 USA; 2Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114 USA Arabidopsis thaliana BAC T07M07 encoding the abscisic acid-insensitive 4 (ABI4) locus has been sequenced completely. It contains a 95,713-bp insert and 24 predicted genes. Most putative genes were confirmed by gel-based RNA profiling and a cluster of ABA-regulated genes was identified. One of the 24 genes, designated PP2C5, encodes a putative protein phosphatase 2C. The encoded protein was expressed in Escherichia coli, and its enzyme activity in vitro was confirmed. [The sequence data described in this paper have been submitted to GenBank under accession no. AF085279.] Sequencing the entire genomes of model organisms is Burge and Karlin 1997) were used for gene prediction. fundamentally shifting the way we study gene expres- Prior to functional studies, a gel-based RNA profiling sion and function. Traditionally, the search for gene method was used to confirm whether these putative function started with a phenotypic mutant and pro- genes were indeed expressed. In general, the model ceeded to gene cloning and functional analysis—“from that emerged by comparison of all the predictions was phenotype to gene”. Now, as genome sequencing is in good agreement with the experimental data.
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