Anti-Crkii Antibody (ARG57859)

Total Page：16

File Type：pdf, Size：1020Kb

Product datasheet [email protected] ARG57859 Package: 50 μl anti-CrkII antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes CrkII Tested Reactivity Hu Tested Application WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name CrkII Antigen Species Human Immunogen Recombinant protein of Human CrkII. Conjugation Un-conjugated Alternate Names CRKII; p38; Proto-oncogene c-Crk; Adapter molecule crk Application Instructions Application table Application Dilution WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control HepG2 Calculated Mw 34 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol CRK Gene Full Name v-crk avian sarcoma virus CT10 oncogene homolog Background This gene encodes a member of an adapter protein family that binds to several tyrosine- phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described. [provided by RefSeq, Jul 2008] Function The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk- I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac- dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling. [UniProt] Cellular Localization Cytoplasm, Cell membrane. [UniProt] Images ARG57859 anti-CrkII antibody WB image Western blot: 25 µg of HepG2 cell lysate stained with ARG57859 anti- CrkII antibody. www.arigobio.com 2/2 Powered by TCPDF (www.tcpdf.org).

Copy Link

Recommended publications

The Atypical Guanine-Nucleotide Exchange Factor, Dock7, Negatively Regulates Schwann Cell Differentiation and Myelination
The Journal of Neuroscience, August 31, 2011 • 31(35):12579–12592 • 12579 Cellular/Molecular The Atypical Guanine-Nucleotide Exchange Factor, Dock7, Negatively Regulates Schwann Cell Differentiation and Myelination Junji Yamauchi,1,3,5 Yuki Miyamoto,1 Hajime Hamasaki,1,3 Atsushi Sanbe,1 Shinji Kusakawa,1 Akane Nakamura,2 Hideki Tsumura,2 Masahiro Maeda,4 Noriko Nemoto,6 Katsumasa Kawahara,5 Tomohiro Torii,1 and Akito Tanoue1 1Department of Pharmacology and 2Laboratory Animal Resource Facility, National Research Institute for Child Health and Development, Setagaya, Tokyo 157-8535, Japan, 3Department of Biological Sciences, Tokyo Institute of Technology, Midori, Yokohama 226-8501, Japan, 4IBL, Ltd., Fujioka, Gumma 375-0005, Japan, and 5Department of Physiology and 6Bioimaging Research Center, Kitasato University School of Medicine, Sagamihara, Kanagawa 252-0374, Japan In development of the peripheral nervous system, Schwann cells proliferate, migrate, and ultimately differentiate to form myelin sheath. In all of the myelination stages, Schwann cells continuously undergo morphological changes; however, little is known about their underlying molecular mechanisms. We previously cloned the dock7 gene encoding the atypical Rho family guanine-nucleotide exchange factor (GEF) and reported the positive role of Dock7, the target Rho GTPases Rac/Cdc42, and the downstream c-Jun N-terminal kinase in Schwann cell migration (Yamauchi et al., 2008). We investigated the role of Dock7 in Schwann cell differentiation and myelination. Knockdown of Dock7 by the specific small interfering (si)RNA in primary Schwann cells promotes dibutyryl cAMP-induced morpholog- ical differentiation, indicating the negative role of Dock7 in Schwann cell differentiation. It also results in a shorter duration of activation of Rac/Cdc42 and JNK, which is the negative regulator of myelination, and the earlier activation of Rho and Rho-kinase, which is the positive regulator of myelination.
[Show full text]
Related Malignant Phenotypes in the Nf1-Deficient MPNST
Published OnlineFirst February 19, 2013; DOI: 10.1158/1541-7786.MCR-12-0593 Molecular Cancer Genomics Research RAS/MEK–Independent Gene Expression Reveals BMP2- Related Malignant Phenotypes in the Nf1-Deficient MPNST Daochun Sun1, Ramsi Haddad2,3, Janice M. Kraniak2, Steven D. Horne1, and Michael A. Tainsky1,2 Abstract Malignant peripheral nerve sheath tumor (MPNST) is a type of soft tissue sarcoma that occurs in carriers of germline mutations in Nf1 gene as well as sporadically. Neurofibromin, encoded by the Nf1 gene, functions as a GTPase-activating protein (GAP) whose mutation leads to activation of wt-RAS and mitogen-activated protein kinase (MAPK) signaling in neurofibromatosis type I (NF1) patients' tumors. However, therapeutic targeting of RAS and MAPK have had limited success in this disease. In this study, we modulated NRAS, mitogen-activated protein/extracellular signal–regulated kinase (MEK)1/2, and neurofibromin levels in MPNST cells and determined gene expression changes to evaluate the regulation of signaling pathways in MPNST cells. Gene expression changes due to neurofibromin modulation but independent of NRAS and MEK1/2 regulation in MPNST cells indicated bone morphogenetic protein 2 (Bmp2) signaling as a key pathway. The BMP2-SMAD1/5/8 pathway was activated in NF1-associated MPNST cells and inhibition of BMP2 signaling by LDN-193189 or short hairpin RNA (shRNA) to BMP2 decreased the motility and invasion of NF1-associated MPNST cells. The pathway-specific gene changes provide a greater understanding of the complex role of neurofibromin in MPNST pathology and novel targets for drug discovery. Mol Cancer Res; 11(6); 616–27.
[Show full text]
A Rac/Cdc42 Exchange Factor Complex Promotes Formation of Lateral filopodia and Blood Vessel Lumen Morphogenesis
ARTICLE Received 1 Oct 2014 | Accepted 26 Apr 2015 | Published 1 Jul 2015 DOI: 10.1038/ncomms8286 OPEN A Rac/Cdc42 exchange factor complex promotes formation of lateral filopodia and blood vessel lumen morphogenesis Sabu Abraham1,w,*, Margherita Scarcia2,w,*, Richard D. Bagshaw3,w,*, Kathryn McMahon2,w, Gary Grant2, Tracey Harvey2,w, Maggie Yeo1, Filomena O.G. Esteves2, Helene H. Thygesen2,w, Pamela F. Jones4, Valerie Speirs2, Andrew M. Hanby2, Peter J. Selby2, Mihaela Lorger2, T. Neil Dear4,w, Tony Pawson3,z, Christopher J. Marshall1 & Georgia Mavria2 During angiogenesis, Rho-GTPases influence endothelial cell migration and cell–cell adhesion; however it is not known whether they control formation of vessel lumens, which are essential for blood flow. Here, using an organotypic system that recapitulates distinct stages of VEGF-dependent angiogenesis, we show that lumen formation requires early cytoskeletal remodelling and lateral cell–cell contacts, mediated through the RAC1 guanine nucleotide exchange factor (GEF) DOCK4 (dedicator of cytokinesis 4). DOCK4 signalling is necessary for lateral filopodial protrusions and tubule remodelling prior to lumen formation, whereas proximal, tip filopodia persist in the absence of DOCK4. VEGF-dependent Rac activation via DOCK4 is necessary for CDC42 activation to signal filopodia formation and depends on the activation of RHOG through the RHOG GEF, SGEF. VEGF promotes interaction of DOCK4 with the CDC42 GEF DOCK9. These studies identify a novel Rho-family GTPase activation cascade for the formation of endothelial cell filopodial protrusions necessary for tubule remodelling, thereby influencing subsequent stages of lumen morphogenesis. 1 Institute of Cancer Research, Division of Cancer Biology, 237 Fulham Road, London SW3 6JB, UK.
[Show full text]
Anti-CRK Monoclonal Antibody, Clone 4H22D2 (DCABH-1226) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-CRK monoclonal antibody, clone 4H22D2 (DCABH-1226) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Mouse monoclonal to Crk p38 Antigen Description The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. Immunogen Purified recombinant fragment of Human Crk p38 expressed in E. Coli. Isotype IgG2b Source/Host Mouse Species Reactivity Mouse, Human Clone 4H22D2 Purity Ascites Conjugate Unconjugated Applications WB, ELISA, IHC-P, Flow Cyt, ICC/IF Positive Control Recombinant Crk p38 protein; Crk p38-hIgGFc transfected HEK293 cell lysate; Human rectum cancer and bladder cancer tissues; MCF7 and 3T3 L1 cells. Format Liquid Size 100 μl Buffer Preservative: 0.03% Sodium azide; Constituent: 99% Ascites Preservative 0.03% Sodium Azide Storage Store at 4°C or at -20°C for long term storage. GENE INFORMATION 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Gene Name CRK v-crk sarcoma virus CT10 oncogene homolog (avian) [ Homo sapiens ] Official Symbol CRK Synonyms CRK; v-crk sarcoma virus CT10 oncogene homolog (avian); v crk avian sarcoma virus CT10 oncogene homolog; adapter molecule crk; proto-oncogene
[Show full text]
Breast Cancer Antiestrogen Resistance-3 Expression Regulates Breast Cancer Cell Migration Through Promotion of P130cas Membrane Localization Andmembrane Ruffling
Research Article Breast Cancer Antiestrogen Resistance-3 Expression Regulates Breast Cancer Cell Migration through Promotion of p130Cas Membrane Localization andMembrane Ruffling Randy S. Schrecengost,1 Rebecca B. Riggins,2 Keena S. Thomas,1 Michael S. Guerrero,1 and Amy H. Bouton1 1Department of Microbiology, University of Virginia Health System, Charlottesville, Virginia and 2Department of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, District of Columbia Abstract antiestrogen resistance-1 (BCAR1; also known as p130Cas; refs. 2, 3). Antiestrogens such as tamoxifen are widely used in the clinic A second protein, BCAR3 (the human homologue of the murine to treat estrogen receptor–positive breast tumors. Resistance protein AND-34), was identified in a genetic screen along with to tamoxifen can occur either de novo or develop over time in BCAR1 as a gene product whose overexpression conferred tamoxifen resistance in vitro (4). BCAR3 is a member of the novel a large proportion of these tumors. Additionally, resistance is S p associated with enhanced motility and invasiveness in vitro. rc homology 2 (SH2)–containing rotein (NSP) family that One molecule that has been implicated in tamoxifen resis- includes two other members, Chat/SHEP1 and NSP1. These tance, breast cancer antiestrogen resistance-3 (BCAR3), has proteins share a common domain structure consisting of an also been shown to regulate migration of fibroblasts. In this amino-terminal SH2 domain and a carboxyl-terminal domain with study, we investigated the role of BCAR3 in breast cancer cell sequence homology to the Cdc25-family of guanine nucleotide exchange factors (GEF). Several studies have shown that BCAR3 migration and invasion.
[Show full text]
A Rhog-Mediated Signaling Pathway That Modulates Invadopodia Dynamics in Breast Cancer Cells Silvia M
© 2017. Published by The Company of Biologists Ltd | Journal of Cell Science (2017) 130, 1064-1077 doi:10.1242/jcs.195552 RESEARCH ARTICLE A RhoG-mediated signaling pathway that modulates invadopodia dynamics in breast cancer cells Silvia M. Goicoechea, Ashtyn Zinn, Sahezeel S. Awadia, Kyle Snyder and Rafael Garcia-Mata* ABSTRACT micropinocytosis, bacterial uptake, phagocytosis and leukocyte One of the hallmarks of cancer is the ability of tumor cells to invade trans-endothelial migration (deBakker et al., 2004; Ellerbroek et al., surrounding tissues and metastasize. During metastasis, cancer cells 2004; Jackson et al., 2015; Katoh et al., 2006, 2000; van Buul et al., degrade the extracellular matrix, which acts as a physical barrier, by 2007). Recent studies have revealed that RhoG plays a role in tumor developing specialized actin-rich membrane protrusion structures cell invasion and may contribute to the formation of invadopodia called invadopodia. The formation of invadopodia is regulated by Rho (Hiramoto-Yamaki et al., 2010; Kwiatkowska et al., 2012). GTPases, a family of proteins that regulates the actin cytoskeleton. Invadopodia are actin-rich adhesive structures that form in the Here, we describe a novel role for RhoG in the regulation of ventral surface of cancer cells and allow them to degrade the invadopodia disassembly in human breast cancer cells. Our results extracellular matrix (ECM) (Gimona et al., 2008). Formation of show that RhoG and Rac1 have independent and opposite roles invadopodia involves a series of steps that include the disassembly in the regulation of invadopodia dynamics. We also show that SGEF of focal adhesions and stress fibers, and the relocalization of several (also known as ARHGEF26) is the exchange factor responsible of their components into the newly formed invadopodia (Hoshino for the activation of RhoG during invadopodia disassembly.
[Show full text]
Dock3 Stimulates Axonal Outgrowth Via GSK-3ß-Mediated Microtubule
264 • The Journal of Neuroscience, January 4, 2012 • 32(1):264–274 Development/Plasticity/Repair Dock3 Stimulates Axonal Outgrowth via GSK-3␤-Mediated Microtubule Assembly Kazuhiko Namekata, Chikako Harada, Xiaoli Guo, Atsuko Kimura, Daiji Kittaka, Hayaki Watanabe, and Takayuki Harada Visual Research Project, Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan Dock3, a new member of the guanine nucleotide exchange factors, causes cellular morphological changes by activating the small GTPase Rac1. Overexpression of Dock3 in neural cells promotes axonal outgrowth downstream of brain-derived neurotrophic factor (BDNF) signaling. We previously showed that Dock3 forms a complex with Fyn and WASP (Wiskott–Aldrich syndrome protein) family verprolin- homologous (WAVE) proteins at the plasma membrane, and subsequent Rac1 activation promotes actin polymerization. Here we show that Dock3 binds to and inactivates glycogen synthase kinase-3␤ (GSK-3␤) at the plasma membrane, thereby increasing the nonphos- phorylated active form of collapsin response mediator protein-2 (CRMP-2), which promotes axon branching and microtubule assembly. Exogenously applied BDNF induced the phosphorylation of GSK-3␤ and dephosphorylation of CRMP-2 in hippocampal neurons. More- over, increased phosphorylation of GSK-3␤ was detected in the regenerating axons of transgenic mice overexpressing Dock3 after optic nerve injury. These results suggest that Dock3 plays important roles downstream of BDNF signaling in the CNS, where it regulates cell polarity and promotes axonal outgrowth by stimulating dual pathways: actin polymerization and microtubule assembly. Introduction We recently detected a common active center of Dock1ϳ4 within The Rho-GTPases, including Rac1, Cdc42, and RhoA, are best the DHR-2 domain and reported that the DHR-1 domain is nec- known for their roles in regulating the actin cytoskeleton and are essary for the direct binding between Dock1ϳ4 and WAVE1ϳ3 implicated in a broad spectrum of biological functions, such as (Namekata et al., 2010).
[Show full text]
Physiological Signaling and Structure of the HGF Receptor MET
Biomedicines 2015, 3, 1-31; doi:10.3390/biomedicines3010001 OPEN ACCESS biomedicines ISSN 2227-9059 www.mdpi.com/journal/biomedicines/ Review Physiological Signaling and Structure of the HGF Receptor MET Gianluca Baldanzi 1,* and Andrea Graziani 1,2 1 Department Translational Medicine, University Piemonte Orientale, via Solaroli 17, 28100 Novara, Italy 2 Università Vita-Salute San Raffaele, via Olgettina 58, 20132 Milano, Italy; E-Mail: [email protected] * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +39-0321-660527; Fax: +39-0321-620421. Academic Editor: Zimmer Yitzhak Received: 30 September 2014 / Accepted: 9 December 2014 / Published: 31 December 2014 Abstract: The “hepatocyte growth factor” also known as “scatter factor”, is a multifunctional cytokine with the peculiar ability of simultaneously triggering epithelial cell proliferation, movement and survival. The combination of those proprieties results in the induction of an epithelial to mesenchymal transition in target cells, fundamental for embryogenesis but also exploited by tumor cells during metastatization. The hepatocyte growth factor receptor, MET, is a proto-oncogene and a prototypical transmembrane tyrosine kinase receptor. Inhere we discuss the MET molecular structure and the hepatocyte growth factor driven physiological signaling which coordinates epithelial proliferation, motility and morphogenesis. Keywords: signaling pathways; tyrosine kinase receptor; protein–protein interaction; SH2 domain; post translational modification; signal transduction 1. Background Introduction The Hepatocyte Growth Factor (HGF) was originally identified as a soluble factor promoting hepatocyte growth and liver regeneration [1]. In a parallel way a Scatter Factor (SF) was identified as cytokine secreted by fibroblast promoting dissociation and motility of epithelial cells in culture [2].
[Show full text]
The Extracellular Matrix for Bone Regeneration
This chapter is based on human mesenchymal stromal cells in adhesion to cell-derived 5 extracellular matrix and titanium: a comparative kinome profi le analysis Marta Baroncelli1^, Gwenny M. Fuhler2^, Jeroen van de Peppel1, Willian F. Zambuzzi3, Johannes P.T.M van Leeuwen1, Bram C.J van der Eerden1°, Maikel P. Peppelenbosch2° 1Department of Internal Medicine, Erasmus MC. University Medical Center Rotterdam, Wytemaweg 80, 3015 CN, Rotterdam, The Netherlands 2Department of Gastroenterology and Hepatology, Erasmus MC, University Medical Center Rotterdam, Wytemaweg 80, 3015 CN, Rotterdam, The Netherlands 3Laboratorio de Bioensaios e Dinâmica Celular, Dep.to de Quimica e Bioquimica, Instituto de Biociências, Universidade Estadual Paulista- UNESP, Campus Botucatu, São Paulo, SP Brazil. ^, °: both authors contributed equally to this work Submitted Chapter 5 ABSTRACT The extracellular matrix (ECM) is an essential component of tissue architecture that physically supports cells and actively influences stem cell behaviour, by modulating kinase-mediated signaling cascades that are the key regulators of signal transduc- tion. Cell-derived ECMs have recently emerged in the context of bone regeneration, as they reproduce physiological tissue-architecture and ameliorate the promising properties of mesenchymal stromal cells (MSCs). Titanium scaffolds show good mechanical properties and porosity to facilitate cell adhesion, and thus have been routinely used for bone tissue engineering applications. The aim of this study was to analyze the kinomic signature of human MSCs in adhesion to an osteoblast-derived ECM that we have previously shown to be osteopromotive, and to compare it to MSCs on titanium. PamChip kinase array analysis revealed 63 phosphorylated peptides on ECM and 59 on titanium, with MSCs on ECM exhibiting significant higher levels of kinase activity than those on titanium.
[Show full text]
Identification of Transcriptional Mechanisms Downstream of Nf1 Gene Defeciency in Malignant Peripheral Nerve Sheath Tumors Daochun Sun Wayne State University
Wayne State University DigitalCommons@WayneState Wayne State University Dissertations 1-1-2012 Identification of transcriptional mechanisms downstream of nf1 gene defeciency in malignant peripheral nerve sheath tumors Daochun Sun Wayne State University, Follow this and additional works at: http://digitalcommons.wayne.edu/oa_dissertations Recommended Citation Sun, Daochun, "Identification of transcriptional mechanisms downstream of nf1 gene defeciency in malignant peripheral nerve sheath tumors" (2012). Wayne State University Dissertations. Paper 558. This Open Access Dissertation is brought to you for free and open access by DigitalCommons@WayneState. It has been accepted for inclusion in Wayne State University Dissertations by an authorized administrator of DigitalCommons@WayneState. IDENTIFICATION OF TRANSCRIPTIONAL MECHANISMS DOWNSTREAM OF NF1 GENE DEFECIENCY IN MALIGNANT PERIPHERAL NERVE SHEATH TUMORS by DAOCHUN SUN DISSERTATION Submitted to the Graduate School of Wayne State University, Detroit, Michigan in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY 2012 MAJOR: MOLECULAR BIOLOGY AND GENETICS Approved by: _______________________________________ Advisor Date _______________________________________ _______________________________________ _______________________________________ © COPYRIGHT BY DAOCHUN SUN 2012 All Rights Reserved DEDICATION This work is dedicated to my parents and my wife Ze Zheng for their continuous support and understanding during the years of my education. I could not achieve my goal without them. ii ACKNOWLEDGMENTS I would like to express tremendous appreciation to my mentor, Dr. Michael Tainsky. His guidance and encouragement throughout this project made this dissertation come true. I would also like to thank my committee members, Dr. Raymond Mattingly and Dr. John Reiners Jr. for their sustained attention to this project during the monthly NF1 group meetings and committee meetings, Dr.
[Show full text]
Molecular Signatures Differentiate Immune States in Type 1 Diabetes Families
Page 1 of 65 Diabetes Molecular signatures differentiate immune states in Type 1 diabetes families Yi-Guang Chen1, Susanne M. Cabrera1, Shuang Jia1, Mary L. Kaldunski1, Joanna Kramer1, Sami Cheong2, Rhonda Geoffrey1, Mark F. Roethle1, Jeffrey E. Woodliff3, Carla J. Greenbaum4, Xujing Wang5, and Martin J. Hessner1 1The Max McGee National Research Center for Juvenile Diabetes, Children's Research Institute of Children's Hospital of Wisconsin, and Department of Pediatrics at the Medical College of Wisconsin Milwaukee, WI 53226, USA. 2The Department of Mathematical Sciences, University of Wisconsin-Milwaukee, Milwaukee, WI 53211, USA. 3Flow Cytometry & Cell Separation Facility, Bindley Bioscience Center, Purdue University, West Lafayette, IN 47907, USA. 4Diabetes Research Program, Benaroya Research Institute, Seattle, WA, 98101, USA. 5Systems Biology Center, the National Heart, Lung, and Blood Institute, the National Institutes of Health, Bethesda, MD 20824, USA. Corresponding author: Martin J. Hessner, Ph.D., The Department of Pediatrics, The Medical College of Wisconsin, Milwaukee, WI 53226, USA Tel: 011-1-414-955-4496; Fax: 011-1-414-955-6663; E-mail: [email protected]. Running title: Innate Inflammation in T1D Families Word count: 3999 Number of Tables: 1 Number of Figures: 7 1 For Peer Review Only Diabetes Publish Ahead of Print, published online April 23, 2014 Diabetes Page 2 of 65 ABSTRACT Mechanisms associated with Type 1 diabetes (T1D) development remain incompletely defined. Employing a sensitive array-based bioassay where patient plasma is used to induce transcriptional responses in healthy leukocytes, we previously reported disease-specific, partially IL-1 dependent, signatures associated with pre and recent onset (RO) T1D relative to unrelated healthy controls (uHC).
[Show full text]
SUPPLEMENTAL MATERIAL TGF-Β/Smad Signaling Through DOCK4 Facilitates Lung Adenocarcinoma Metastasis Ten Supplemental Figures Fo
SUPPLEMENTAL MATERIAL TGF-β/Smad signaling through DOCK4 facilitates lung adenocarcinoma metastasis Jia-Ray Yu, Yilin Tai, Ying Jin, Molly C. Hammell, J. Erby Wilkinson, Jae-Seok Roe, Christopher R. Vakoc, and Linda Van Aelst Ten Supplemental Figures Four Supplemental Tables Supplemental Materials and Methods Supplemental References Supplemental Figure 1, related to Figure 1. TGF-β/Smad signaling induces DOCK4 expression in lung ADC cells, but not breast cancer cells. (A) Heat map showing differential expression of all 83 Rho family GEFs in TGF-β treated A549 cells over a 72- h time window. Gene expression data are presented on a log2 scale. Blue and yellow indicate upregulation and downregulation, respectively, by TGF-β. The top 21 TGF-β upregulated Rho family-GEFs are listed on the right. Original data were retrieved from Gene Expression Omnibus (GEO) with accession number GSE17708. (B) Western blot analysis of DOCK4, p-Smad3, and Smad3 in a panel of breast cancer cell lines treated with 2 ng/ml TGF-β over a 3-d time window. Gapdh was used as a loading control. (C) Western blot analysis of DOCK4, p-β-catenin, and β-catenin in A549 cells treated with 100 ng/ml WNT3A over a 2-d time window. (D) Western blot analysis of DOCK4 and Smad4 in shCtrl- and shSmad4#2-expressing A549 cells treated with 2 ng/ml TGF-β over a 2-d time window. Asterisk depicts a non-specific band. (E) Western blot analysis of DOCK4 and E-cadherin in shCtrl- and shSmad4#1-expressing HCC4006 cells treated with 2 ng/ml TGF-β over a 3-d time window.
[Show full text]