IGFBP4 Antibody

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Product Datasheet IGFBP4 antibody Catalog No: #38333 Orders: [email protected] Description Support: [email protected] Product Name IGFBP4 antibody Host Species Rabbit Clonality Polyclonal Purification Antibodies were purified by affinity purification using immunogen. Applications WB,IHC,IF Species Reactivity Human,Mouse,Rat Specificity The antibody detects endogenous level of total IGFBP4 antibody. Immunogen Type Recombinant Protein Immunogen Description Recombinant protein of human IGFBP4. Target Name IGFBP4 Other Names BP-4; IBP4; IGFBP-4; HT29-IGFBP; Accession No. Swiss-Prot#: P22692NCBI Gene ID: 3487 SDS-PAGE MW 28kd Concentration 1.0mg/ml Formulation Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Storage Store at -20°C Application Details WB 1:500 - 1:2000IHC 1:50 - 1:100IF 1:50 - 1:200 Images Immunofluorescence analysis of L929 cells using IGFBP4 at dilution of 1:100. Blue: DAPI for nuclear staining. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 1 Immunohistochemistry of paraffin-embedded rat brain using IGFBP4 at dilution of 1:100 (40x lens). Immunohistochemistry of paraffin-embedded human stomach using IGFBP4 at dilution of 1:100 (40x lens). Western blot analysis of extracts of various cell lines, using IGFBP4 at 1:1000 dilution. Immunohistochemistry of paraffin-embedded mouse brain using IGFBP4 at dilution of 1:100 (40x lens). Background This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma in both glycosylated and non-glycosylated forms. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 2 Note: This product is for in vitro research use only and is not intended for use in humans or animals. Address: 8400 Baltimore Ave., Suite 302, College Park, MD 20740, USA http://www.sabbiotech.com 3.

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Endothelial Cells and the IGF System
L A Bach Endothelial cells as IGF targets 54:1 R1–R13 Review Endothelial cells and the IGF system Correspondence 1,2 Leon A Bach should be addressed to L A Bach 1Department of Medicine (Alfred), Monash University, Prahran 3181, Australia Email 2Department of Endocrinology and Diabetes, Alfred Hospital, Commercial Road, Melbourne 3004, Australia [email protected] Abstract Endothelial cells line blood vessels and modulate vascular tone, thrombosis, inflammatory Key Words responses and new vessel formation. They are implicated in many disease processes including " insulin-like growth factor atherosclerosis and cancer. IGFs play a significant role in the physiology of endothelial cells " binding protein by promoting migration, tube formation and production of the vasodilator nitric oxide. " receptor These actions are mediated by the IGF1 and IGF2/mannose 6-phosphate receptors and are " endothelial cell modulated by a family of high-affinity IGF binding proteins. IGFs also increase the number " angiogenesis and function of endothelial progenitor cells, which may contribute to protection from atherosclerosis. IGFs promote angiogenesis, and dysregulation of the IGF system may contribute to this process in cancer and eye diseases including retinopathy of prematurity and diabetic retinopathy. In some situations, IGF deficiency appears to contribute to endothelial dysfunction, whereas IGF may be deleterious in others. These differences may be due to tissue-specific endothelial cell phenotypes or IGFs having distinct roles in different phases of vascular disease. Further studies are therefore required to delineate the Journal of Molecular therapeutic potential of IGF system modulation in pathogenic processes. Endocrinology (2015) 54, R1–R13 Journal of Molecular Endocrinology Introduction Insulin-like growth factor 1 (IGF1) and IGF2 are essential metabolically active and regulate vascular tone, thrombosis, for normal pre- and postnatal growth and development inflammatory responses and new vessel formation.
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Insulin-Like Growth Factor Axis in Pregnancies Affected by Fetal Growth Disorders Aamod R
Nawathe et al. Clinical Epigenetics (2016) 8:11 DOI 10.1186/s13148-016-0178-5 RESEARCH Open Access Insulin-like growth factor axis in pregnancies affected by fetal growth disorders Aamod R. Nawathe1,2, Mark Christian3, Sung Hye Kim2, Mark Johnson1,2, Makrina D. Savvidou1,2 and Vasso Terzidou1,2* Abstract Background: Insulin-like growth factors 1 and 2 (IGF1 and IGF2) and their binding proteins (IGFBPs) are expressed in the placenta and known to regulate fetal growth. DNA methylation is an epigenetic mechanism which involves addition of methyl group to a cytosine base in the DNA forming a methylated cytosine-phosphate-guanine (CpG) dinucleotide which is known to silence gene expression. This silences gene expression, potentially altering the expression of IGFs and their binding proteins. This study investigates the relationship between DNA methylation of components of the IGF axis in the placenta and disorders in fetal growth. Placental samples were obtained from cord insertions immediately after delivery from appropriate, small (defined as birthweight <10th percentile for the gestation [SGA]) and macrosomic (defined as birthweight > the 90th percentile for the gestation [LGA]) neonates. Placental DNA methylation, mRNA expression and protein levels of components of the IGF axis were determined by pyrosequencing, rtPCR and Western blotting. Results: In the placenta from small for gestational age (SGA) neonates (n = 16), mRNA and protein levels of IGF1 were lower and of IGFBPs (1, 2, 3, 4 and 7) were higher (p < 0.05) compared to appropriately grown neonates (n =37).In contrast, in the placenta from large for gestational age (LGA) neonates (n = 20), mRNA and protein levels of IGF1 was not different and those of IGFBPs (1, 2, 3 and 4) were lower (p < 0.05) compared to appropriately grown neonates.
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Supplementary Table 1: Genes Affected by Anoikis. A, Ratio of Signal
Supplementary Table 1: Genes affected by anoikis. a, ratio of signal intensity of nonanchored cells anchorage dependent cells (CasKoSrc) over anchored cells; b, induced by Src transformation of Cx43KO cells; c, decreased by Src transformation of Cx43Ko cells; *, induced by normalization of Src transformed cells by neighboring nontransformed cells. Gene Symbol Probe Set Fold Changea Gene Name increased Selenbp1 1450699_at 23.22 selenium binding protein 1 Dscr1l1 1450243_a_at 10.77 Down syndrome critical region gene 1-like 1 Dscr1l1 1421425_a_at 4.29 Down syndrome critical region gene 1-like 1 Ttyh1 1426617_a_at 6.70 tweety homolog 1 (Drosophila) 5730521E12Rik 1419065_at 6.16 RIKEN cDNA 5730521E12 gene c 6330406I15Rik 1452244_at 5.87 RIKEN cDNA 6330406I15 gene AF067063 1425160_at 5.73 clone L2 uniform group of 2-cell-stage gene family mRNA Morc 1419418_a_at 5.55 microrchidia c Gpr56 1421118_a_at 5.43 G protein-coupled receptor 56 Pax6 1452526_a_at 5.06 paired box gene 6 Tgfbi 1415871_at 3.73 transforming growth factor beta induced Adarb1 1434932_at 3.70 adenosine deaminase RNA-specific B1 Ddx3y 1452077_at 3.30 DEAD (Asp-Glu-Ala-Asp) box polypeptide 3 Y-linked b Ampd3 1422573_at 3.20 AMP deaminase 3 Gli2 1459211_at 3.07 GLI-Kruppel family member GLI2 Selenbp2 1417580_s_at 2.96 selenium binding protein 2 Adamts1 1450716_at 2.80 a disintegrin-like and metalloprotease with thrombospondin type 1 motif 1 Dusp15 1426189_at 2.70 dual specificity phosphatase-like 15 Dpep3 1429035_at 2.60 dipeptidase 3 Sepp1 1452141_a_at 2.57 selenoprotein P plasma
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Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................
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Trim24-Regulated Estrogen Response Is Dependent on Specific Histone Modifications in Breast Cancer Cells
The Texas Medical Center Library DigitalCommons@TMC The University of Texas MD Anderson Cancer Center UTHealth Graduate School of The University of Texas MD Anderson Cancer Biomedical Sciences Dissertations and Theses Center UTHealth Graduate School of (Open Access) Biomedical Sciences 12-2012 TRIM24-REGULATED ESTROGEN RESPONSE IS DEPENDENT ON SPECIFIC HISTONE MODIFICATIONS IN BREAST CANCER CELLS Teresa T. Yiu Follow this and additional works at: https://digitalcommons.library.tmc.edu/utgsbs_dissertations Part of the Biochemistry Commons, Cancer Biology Commons, Medicine and Health Sciences Commons, and the Molecular Biology Commons Recommended Citation Yiu, Teresa T., "TRIM24-REGULATED ESTROGEN RESPONSE IS DEPENDENT ON SPECIFIC HISTONE MODIFICATIONS IN BREAST CANCER CELLS" (2012). The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access). 313. https://digitalcommons.library.tmc.edu/utgsbs_dissertations/313 This Dissertation (PhD) is brought to you for free and open access by the The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at DigitalCommons@TMC. It has been accepted for inclusion in The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access) by an authorized administrator of DigitalCommons@TMC. For more information, please contact [email protected]. TRIM24-REGULATED ESTROGEN RESPONSE IS DEPENDENT ON SPECIFIC HISTONE
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Citation: Cell Death and Disease (2013) 4, e911; doi:10.1038/cddis.2013.445 OPEN & 2013 Macmillan Publishers Limited All rights reserved 2041-4889/13 www.nature.com/cddis Insulin-like growth factor binding proteins 4 and 7 released by senescent cells promote premature senescence in mesenchymal stem cells V Severino1,2,3,10, N Alessio4,10, A Farina5, A Sandomenico2,3, M Cipollaro4, G Peluso6,7, U Galderisi*,4,6,8,9 and A Chambery*,1,3 Cellular senescence is the permanent arrest of cell cycle, physiologically related to aging and aging-associated diseases. Senescence is also recognized as a mechanism for limiting the regenerative potential of stem cells and to protect cells from cancer development. The senescence program is realized through autocrine/paracrine pathways based on the activation of a peculiar senescence-associated secretory phenotype (SASP). We show here that conditioned media (CM) of senescent mesenchymal stem cells (MSCs) contain a set of secreted factors that are able to induce a full senescence response in young cells. To delineate a hallmark of stem cells SASP, we have characterized the factors secreted by senescent MSC identifying insulin-like growth factor binding proteins 4 and 7 (IGFBP4 and IGFBP7) as key components needed for triggering senescence in young MSC. The pro-senescent effects of IGFBP4 and IGFBP7 are reversed by single or simultaneous immunodepletion of either proteins from senescent-CM. The blocking of IGFBP4/7 also reduces apoptosis and promotes cell growth, suggesting that they may have a pleiotropic effect on MSC biology. Furthermore, the simultaneous addition of rIGFBP4/7 increased senescence and induced apoptosis in young MSC.
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bioRxiv preprint doi: https://doi.org/10.1101/2021.02.23.432411; this version posted March 12, 2021. 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. Chromatin reader Dido3 regulates the genetic network of B cell differentiation Fernando Gutiérrez del Burgo1, Tirso Pons1, Enrique Vázquez de Luis2, Carlos Martínez-A1 & Ricardo Villares1,* 1 Centro Nacional de Biotecnología/CSIC, Darwin 3, Cantoblanco, E‐28049, Madrid, Spain 2 Centro Nacional de Investigaciones Cardiovasculares, Instituto de Salud Carlos III, Melchor Fernández Almagro 3, Madrid 28029, Spain. *email: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.02.23.432411; this version posted March 12, 2021. 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. ABSTRACT The development of hematopoietic lineages is based on a complex balance of transcription factors whose expression depends on the epigenetic signatures that characterize each differentiation step. The B cell lineage arises from hematopoietic stem cells through the stepwise silencing of stemness genes and balanced expression of mutually regulated transcription factors, as well as DNA rearrangement. Here we report the impact on B cell differentiation of the lack of DIDO3, a reader of chromatin status, in the mouse hematopoietic compartment.
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Mutation of IGFBP7 Causes Upregulation of BRAF/MEK/ERK Pathway and Familial Retinal Arterial Macroaneurysms
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector REPORT Mutation of IGFBP7 Causes Upregulation of BRAF/MEK/ERK Pathway and Familial Retinal Arterial Macroaneurysms Leen Abu-Saﬁeh,1,10 Emad B. Abboud,2,10 Hisham Alkuraya,1,2,10 Hanan Shamseldin,1 Shamsa Al-Enzi,1 Lama Al-Abdi,1 Mais Hashem,1 Dilek Colak,3 Abdullah Jarallah,4 Hala Ahmad,5 Steve Bobis,5 Georges Nemer,6 Fadi Bitar,7 and Fowzan S. Alkuraya1,8,9,* Insulin-like growth factor binding proteins (IGFBPs) play important physiological functions through the modulation of IGF signaling as well as IGF-independent mechanisms. Despite the established role of IGFs in development, a similar role for the seven known IGFBPs has not been established in humans. Here, we show that an autosomal-recessive syndrome that consists of progressive retinal arterial macro- aneurysms and supravalvular pulmonic stenosis is caused by mutation of IGFBP7. Consistent with the recently established inhibitory role of IGFBP7 on BRAF signaling, the BRAF/MEK/ERK pathway is upregulated in these patients, which may explain why the cardiac phenotype overlaps with other disorders characterized by germline mutations in this pathway. The retinal phenotype appears to be mediated by a role in vascular endothelium, where IGFBP7 is highly expressed. Insulin-like growth factors IGF1 (MIM 147440) and IGF2 type in mice in which individual Igfbps have been knocked (MIM 147470) are signaling polypeptides that are involved out.5,7 Therefore, study of IGFBPs
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Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands That Promote Axonal Growth
Research Article: New Research Development Peripheral Nerve Single-Cell Analysis Identifies Mesenchymal Ligands that Promote Axonal Growth Jeremy S. Toma,1 Konstantina Karamboulas,1,ª Matthew J. Carr,1,2,ª Adelaida Kolaj,1,3 Scott A. Yuzwa,1 Neemat Mahmud,1,3 Mekayla A. Storer,1 David R. Kaplan,1,2,4 and Freda D. Miller1,2,3,4 https://doi.org/10.1523/ENEURO.0066-20.2020 1Program in Neurosciences and Mental Health, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada, 2Institute of Medical Sciences University of Toronto, Toronto, Ontario M5G 1A8, Canada, 3Department of Physiology, University of Toronto, Toronto, Ontario M5G 1A8, Canada, and 4Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5G 1A8, Canada Abstract Peripheral nerves provide a supportive growth environment for developing and regenerating axons and are es- sential for maintenance and repair of many non-neural tissues. This capacity has largely been ascribed to paracrine factors secreted by nerve-resident Schwann cells. Here, we used single-cell transcriptional profiling to identify ligands made by different injured rodent nerve cell types and have combined this with cell-surface mass spectrometry to computationally model potential paracrine interactions with peripheral neurons. These analyses show that peripheral nerves make many ligands predicted to act on peripheral and CNS neurons, in- cluding known and previously uncharacterized ligands. While Schwann cells are an important ligand source within injured nerves, more than half of the predicted ligands are made by nerve-resident mesenchymal cells, including the endoneurial cells most closely associated with peripheral axons. At least three of these mesen- chymal ligands, ANGPT1, CCL11, and VEGFC, promote growth when locally applied on sympathetic axons.
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REVIEW IGF-Binding Protein-4
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