Plastin L (LCP1) Rabbit Polyclonal Antibody – TA350140 | Origene

Total Page：16

File Type：pdf, Size：1020Kb

Plastin L (LCP1) Rabbit Polyclonal Antibody – TA350140 | Origene

OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA350140 Plastin L (LCP1) Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: WB Recommended Dilution: ELISA: 2000-5000, WB: 500-2000 Reactivity: Human, Mouse Host: Rabbit Isotype: IgG Clonality: Polyclonal Immunogen: Fusion protein of human LCP1 Formulation: pH7.4 PBS, 0.05% NaN3, 40% Glyceroln Concentration: lot specific Purification: Antigen affinity purification Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 70 kDa Gene Name: lymphocyte cytosolic protein 1 Database Link: NP_002289 Entrez Gene 18826 MouseEntrez Gene 3936 Human P13796 Background: Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. Plastin 1 (otherwise known as Fimbrin) is a third distinct plastin isoform which is specifically expressed at high levels in the small intestine. The L isoform is expressed only in hemopoietic cell lineages, while the T isoform has been found in all other normal cells of solid tissues that have replicative potential (fibroblasts, endothelial cells, epithelial cells, melanocytes, etc.). Synonyms: CP64; HEL-S-37; L-PLASTIN; LC64P; LPL; PLS2 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 Plastin L (LCP1) Rabbit Polyclonal Antibody – TA350140 Product images: Gel: 6%SDS-PAGE, Lysate: 40 ug, Lane: Raji cells, Primary antibody: (LCP1 Antibody) at dilution 1/300, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 10 seconds This product is to be used for laboratory only. Not for diagnostic or therapeutic use. ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 2 / 2.

Copy Link

Recommended publications

Large-Scale Opening of Utrophints Tandem Calponin Homology (CH
Large-scale opening of utrophin’s tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism Ava Y. Lin, Ewa Prochniewicz, Zachary M. James, Bengt Svensson, and David D. Thomas1 Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455 Edited by James A. Spudich, Stanford University School of Medicine, Stanford, CA, and approved June 20, 2011 (received for review April 21, 2011) We have used site-directed spin labeling and pulsed electron has prevented the development of a reliable structural model for paramagnetic resonance to resolve a controversy concerning the any of these complexes. A major unresolved question concerns structure of the utrophin–actin complex, with implications for the the relative disposition of the tandem CH domains (CH1 and pathophysiology of muscular dystrophy. Utrophin is a homolog of CH2) (9, 10). Crystal structures of the tandem CH domains dystrophin, the defective protein in Duchenne and Becker muscular showed a closed conformation for fimbrin (11) and α-actinin (12), dystrophies, and therapeutic utrophin derivatives are currently but an open conformation for both utrophin (Utr261) (Fig. 1A) being developed. Both proteins have a pair of N-terminal calponin and dystrophin (Dys246) (16). The crystal structure of Utr261 homology (CH) domains that are important for actin binding. suggests that the central helical region connecting CH1 and CH2 Although there is a crystal structure of the utrophin actin-binding is highly flexible. Even for α-actinin, which has a closed crystal domain, electron microscopy of the actin-bound complexes has structure, computational analysis suggests the potential for a high produced two very different structural models, in which the CH do- degree of dynamic flexibility that facilitates actin binding (17).
[Show full text]
Mechanical Forces Induce an Asthma Gene Signature in Healthy Airway Epithelial Cells Ayşe Kılıç1,10, Asher Ameli1,2,10, Jin-Ah Park3,10, Alvin T
www.nature.com/scientificreports OPEN Mechanical forces induce an asthma gene signature in healthy airway epithelial cells Ayşe Kılıç1,10, Asher Ameli1,2,10, Jin-Ah Park3,10, Alvin T. Kho4, Kelan Tantisira1, Marc Santolini 1,5, Feixiong Cheng6,7,8, Jennifer A. Mitchel3, Maureen McGill3, Michael J. O’Sullivan3, Margherita De Marzio1,3, Amitabh Sharma1, Scott H. Randell9, Jefrey M. Drazen3, Jefrey J. Fredberg3 & Scott T. Weiss1,3* Bronchospasm compresses the bronchial epithelium, and this compressive stress has been implicated in asthma pathogenesis. However, the molecular mechanisms by which this compressive stress alters pathways relevant to disease are not well understood. Using air-liquid interface cultures of primary human bronchial epithelial cells derived from non-asthmatic donors and asthmatic donors, we applied a compressive stress and then used a network approach to map resulting changes in the molecular interactome. In cells from non-asthmatic donors, compression by itself was sufcient to induce infammatory, late repair, and fbrotic pathways. Remarkably, this molecular profle of non-asthmatic cells after compression recapitulated the profle of asthmatic cells before compression. Together, these results show that even in the absence of any infammatory stimulus, mechanical compression alone is sufcient to induce an asthma-like molecular signature. Bronchial epithelial cells (BECs) form a physical barrier that protects pulmonary airways from inhaled irritants and invading pathogens1,2. Moreover, environmental stimuli such as allergens, pollutants and viruses can induce constriction of the airways3 and thereby expose the bronchial epithelium to compressive mechanical stress. In BECs, this compressive stress induces structural, biophysical, as well as molecular changes4,5, that interact with nearby mesenchyme6 to cause epithelial layer unjamming1, shedding of soluble factors, production of matrix proteins, and activation matrix modifying enzymes, which then act to coordinate infammatory and remodeling processes4,7–10.
[Show full text]
The Roles of Actin-Binding Domains 1 and 2 in the Calcium-Dependent Regulation of Actin Filament Bundling by Human Plastins
Article The Roles of Actin-Binding Domains 1 and 2 in the Calcium-Dependent Regulation of Actin Filament Bundling by Human Plastins Christopher L. Schwebach 1,2, Richa Agrawal 1, Steffen Lindert 1, Elena Kudryashova 1 and Dmitri S. Kudryashov 1,2 1 - Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA 2 - Molecular, Cellular, and Developmental Biology Program, The Ohio State University, Columbus, OH 43210, USA Correspondence to Dmitri S. Kudryashov: Department of Chemistry and Biochemistry, The Ohio State University, 484 W 12th Ave, 728 Biosciences Building, Columbus, OH 43210, USA. [email protected] http://dx.doi.org/10.1016/j.jmb.2017.06.021 Edited by James Sellers Abstract The actin cytoskeleton is a complex network controlled by a vast array of intricately regulated actin-binding proteins. Human plastins (PLS1, PLS2, and PLS3) are evolutionary conserved proteins that non-covalently crosslink actin filaments into tight bundles. Through stabilization of such bundles, plastins contribute, in an isoform-specific manner, to the formation of kidney and intestinal microvilli, inner ear stereocilia, immune synapses, endocytic patches, adhesion contacts, and invadosomes of immune and cancer cells. All plastins comprise an N-terminal Ca2+-binding regulatory headpiece domain followed by two actin-binding domains (ABD1 and ABD2). Actin bundling occurs due to simultaneous binding of both ABDs to separate actin filaments. Bundling is negatively regulated by Ca2+, but the mechanism of this inhibition remains unknown. In 2+ this study, we found that the bundling abilities of PLS1 and PLS2 were similarly sensitive to Ca (pCa50 ~6.4), whereas PLS3 was less sensitive (pCa50 ~5.9).
[Show full text]
Role of RUNX1 in Aberrant Retinal Angiogenesis Jonathan D
Page 1 of 25 Diabetes Identification of RUNX1 as a mediator of aberrant retinal angiogenesis Short Title: Role of RUNX1 in aberrant retinal angiogenesis Jonathan D. Lam,†1 Daniel J. Oh,†1 Lindsay L. Wong,1 Dhanesh Amarnani,1 Cindy Park- Windhol,1 Angie V. Sanchez,1 Jonathan Cardona-Velez,1,2 Declan McGuone,3 Anat O. Stemmer- Rachamimov,3 Dean Eliott,4 Diane R. Bielenberg,5 Tave van Zyl,4 Lishuang Shen,1 Xiaowu Gai,6 Patricia A. D’Amore*,1,7 Leo A. Kim*,1,4 Joseph F. Arboleda-Velasquez*1 Author affiliations: 1Schepens Eye Research Institute/Massachusetts Eye and Ear, Department of Ophthalmology, Harvard Medical School, 20 Staniford St., Boston, MA 02114 2Universidad Pontificia Bolivariana, Medellin, Colombia, #68- a, Cq. 1 #68305, Medellín, Antioquia, Colombia 3C.S. Kubik Laboratory for Neuropathology, Massachusetts General Hospital, 55 Fruit St., Boston, MA 02114 4Retina Service, Massachusetts Eye and Ear Infirmary, Department of Ophthalmology, Harvard Medical School, 243 Charles St., Boston, MA 02114 5Vascular Biology Program, Boston Children’s Hospital, Department of Surgery, Harvard Medical School, 300 Longwood Ave., Boston, MA 02115 6Center for Personalized Medicine, Children’s Hospital Los Angeles, Los Angeles, 4650 Sunset Blvd, Los Angeles, CA 90027, USA 7Department of Pathology, Harvard Medical School, 25 Shattuck St., Boston, MA 02115 Corresponding authors: Joseph F. Arboleda-Velasquez: [email protected] Ph: (617) 912-2517 Leo Kim: [email protected] Ph: (617) 912-2562 Patricia D’Amore: [email protected] Ph: (617) 912-2559 Fax: (617) 912-0128 20 Staniford St. Boston MA, 02114 † These authors contributed equally to this manuscript Word Count: 1905 Tables and Figures: 4 Diabetes Publish Ahead of Print, published online April 11, 2017 Diabetes Page 2 of 25 Abstract Proliferative diabetic retinopathy (PDR) is a common cause of blindness in the developed world’s working adult population, and affects those with type 1 and type 2 diabetes mellitus.
[Show full text]
The Actin Binding Protein Plastin-3 Is Involved in the Pathogenesis of Acute Myeloid Leukemia
cancers Article The Actin Binding Protein Plastin-3 Is Involved in the Pathogenesis of Acute Myeloid Leukemia Arne Velthaus 1, Kerstin Cornils 2,3, Jan K. Hennigs 1, Saskia Grüb 4, Hauke Stamm 1, Daniel Wicklein 5, Carsten Bokemeyer 1, Michael Heuser 6, Sabine Windhorst 4, Walter Fiedler 1 and Jasmin Wellbrock 1,* 1 Department of Oncology, Hematology and Bone Marrow Transplantation with Division of Pneumology, Hubertus Wald University Cancer Center, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany; [email protected] (A.V.); [email protected] (J.K.H.); [email protected] (H.S.); [email protected] (C.B.); ﬁ[email protected] (W.F.) 2 Department of Pediatric Hematology and Oncology, Division of Pediatric Stem Cell Transplantation and Immunology, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany; [email protected] 3 Research Institute Children’s Cancer Center Hamburg, 20246 Hamburg, Germany 4 Center for Experimental Medicine, Institute of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany; [email protected] (S.G.); [email protected] (S.W.) 5 Department of Anatomy and Experimental Morphology, University Cancer Center, University Medical Center Hamburg-Eppendorf, 20246 Hamburg, Germany; [email protected] 6 Hematology, Hemostasis, Oncology and Stem Cell Transplantation, Hannover Medical School, 20246 Hannover, Germany; [email protected] * Correspondence: [email protected]; Tel.: +49-40-7410-55606 Received: 29 September 2019; Accepted: 25 October 2019; Published: 26 October 2019 Abstract: Leukemia-initiating cells reside within the bone marrow in specialized niches where they undergo complex interactions with their surrounding stromal cells.
[Show full text]
Supplementary Data
Supplementary Fig. 1 A B Responder_Xenograft_ Responder_Xenograft_ NON- NON- Lu7336, Vehicle vs Lu7466, Vehicle vs Responder_Xenograft_ Responder_Xenograft_ Sagopilone, Welch- Sagopilone, Welch- Lu7187, Vehicle vs Lu7406, Vehicle vs Test: 638 Test: 600 Sagopilone, Welch- Sagopilone, Welch- Test: 468 Test: 482 Responder_Xenograft_ NON- Lu7860, Vehicle vs Responder_Xenograft_ Sagopilone, Welch - Lu7558, Vehicle vs Test: 605 Sagopilone, Welch- Test: 333 Supplementary Fig. 2 Supplementary Fig. 3 Supplementary Figure S1. Venn diagrams comparing probe sets regulated by Sagopilone treatment (10mg/kg for 24h) between individual models (Welsh Test ellipse p-value<0.001 or 5-fold change). A Sagopilone responder models, B Sagopilone non-responder models. Supplementary Figure S2. Pathway analysis of genes regulated by Sagopilone treatment in responder xenograft models 24h after Sagopilone treatment by GeneGo Metacore; the most significant pathway map representing cell cycle/spindle assembly and chromosome separation is shown, genes upregulated by Sagopilone treatment are marked with red thermometers. Supplementary Figure S3. GeneGo Metacore pathway analysis of genes differentially expressed between Sagopilone Responder and Non-Responder models displaying –log(p-Values) of most significant pathway maps. Supplementary Tables Supplementary Table 1. Response and activity in 22 non-small-cell lung cancer (NSCLC) xenograft models after treatment with Sagopilone and other cytotoxic agents commonly used in the management of NSCLC Tumor Model Response type
[Show full text]
The Role of Actin Binding Proteins in Cell Motility Elizabeth Ojukwu University of Connecticut - Storrs, [email protected]
University of Connecticut OpenCommons@UConn Honors Scholar Theses Honors Scholar Program Spring 5-6-2012 The Role of Actin Binding Proteins in Cell Motility Elizabeth Ojukwu University of Connecticut - Storrs, [email protected] Follow this and additional works at: https://opencommons.uconn.edu/srhonors_theses Part of the Biology Commons, and the Cell and Developmental Biology Commons Recommended Citation Ojukwu, Elizabeth, "The Role of Actin Binding Proteins in Cell Motility" (2012). Honors Scholar Theses. 271. https://opencommons.uconn.edu/srhonors_theses/271 Ojukwu The Role of Actin Binding Proteins in Cell Motility Elizabeth Ojukwu 1 Ojukwu 2 Ojukwu The Role of Actin Binding Proteins in Cell Motility Elizabeth Ojukwu University Scholar Thesis May 2012 Major Advisor- Dr. David Knecht Honors Advisor- Dr. Adam Zweifach University Scholar Advisors- Dr. Victoria Robinson and Dr. Juliet Lee Department of Molecular and Cell Biology University of Connecticut 3 Ojukwu Table of Contents Abstract . 4 Introduction . 5 I. Overview of Cell Motility . 5 II. Dictyostelium Discoideum as a Model Organism . 6 III. The Role of the Actin Cytoskeleton During Cell Migration . 8 IV. Actin Binding Proteins Regulate Actin Dynamics . 9 V. My Project . 12 Chapter 1. The Effect of Actin Binding Protein Over-Expression on Cell Motility . 15 I. Material and Methods . 15 II. Results . 19 III. Discussion and Future Directions . 22 Chapter 2 Generation and Analysis of Fimbrin Double and Triple Null Mutants . 26 I. Material and Methods . 26 II. Results . 32
[Show full text]
Supp Table 6.Pdf
Supplementary Table 6. Processes associated to the 2037 SCL candidate target genes ID Symbol Entrez Gene Name Process NM_178114 AMIGO2 adhesion molecule with Ig-like domain 2 adhesion NM_033474 ARVCF armadillo repeat gene deletes in velocardiofacial syndrome adhesion NM_027060 BTBD9 BTB (POZ) domain containing 9 adhesion NM_001039149 CD226 CD226 molecule adhesion NM_010581 CD47 CD47 molecule adhesion NM_023370 CDH23 cadherin-like 23 adhesion NM_207298 CERCAM cerebral endothelial cell adhesion molecule adhesion NM_021719 CLDN15 claudin 15 adhesion NM_009902 CLDN3 claudin 3 adhesion NM_008779 CNTN3 contactin 3 (plasmacytoma associated) adhesion NM_015734 COL5A1 collagen, type V, alpha 1 adhesion NM_007803 CTTN cortactin adhesion NM_009142 CX3CL1 chemokine (C-X3-C motif) ligand 1 adhesion NM_031174 DSCAM Down syndrome cell adhesion molecule adhesion NM_145158 EMILIN2 elastin microfibril interfacer 2 adhesion NM_001081286 FAT1 FAT tumor suppressor homolog 1 (Drosophila) adhesion NM_001080814 FAT3 FAT tumor suppressor homolog 3 (Drosophila) adhesion NM_153795 FERMT3 fermitin family homolog 3 (Drosophila) adhesion NM_010494 ICAM2 intercellular adhesion molecule 2 adhesion NM_023892 ICAM4 (includes EG:3386) intercellular adhesion molecule 4 (Landsteiner-Wiener blood group)adhesion NM_001001979 MEGF10 multiple EGF-like-domains 10 adhesion NM_172522 MEGF11 multiple EGF-like-domains 11 adhesion NM_010739 MUC13 mucin 13, cell surface associated adhesion NM_013610 NINJ1 ninjurin 1 adhesion NM_016718 NINJ2 ninjurin 2 adhesion NM_172932 NLGN3 neuroligin
[Show full text]
Cytoskeletal Remodeling in Cancer
biology Review Cytoskeletal Remodeling in Cancer Jaya Aseervatham Department of Ophthalmology, University of Texas Health Science Center at Houston, Houston, TX 77054, USA; [email protected]; Tel.: +146-9767-0166 Received: 15 October 2020; Accepted: 4 November 2020; Published: 7 November 2020 Simple Summary: Cell migration is an essential process from embryogenesis to cell death. This is tightly regulated by numerous proteins that help in proper functioning of the cell. In diseases like cancer, this process is deregulated and helps in the dissemination of tumor cells from the primary site to secondary sites initiating the process of metastasis. For metastasis to be efficient, cytoskeletal components like actin, myosin, and intermediate filaments and their associated proteins should co-ordinate in an orderly fashion leading to the formation of many cellular protrusions-like lamellipodia and filopodia and invadopodia. Knowledge of this process is the key to control metastasis of cancer cells that leads to death in 90% of the patients. The focus of this review is giving an overall understanding of these process, concentrating on the changes in protein association and regulation and how the tumor cells use it to their advantage. Since the expression of cytoskeletal proteins can be directly related to the degree of malignancy, knowledge about these proteins will provide powerful tools to improve both cancer prognosis and treatment. Abstract: Successful metastasis depends on cell invasion, migration, host immune escape, extravasation, and angiogenesis. The process of cell invasion and migration relies on the dynamic changes taking place in the cytoskeletal components; actin, tubulin and intermediate filaments. This is possible due to the plasticity of the cytoskeleton and coordinated action of all the three, is crucial for the process of metastasis from the primary site.
[Show full text]
Current Understanding of the Role of Cytoskeletal Cross-Linkers in the Onset and Development of Cardiomyopathies
International Journal of Molecular Sciences Review Current Understanding of the Role of Cytoskeletal Cross-Linkers in the Onset and Development of Cardiomyopathies Ilaria Pecorari 1, Luisa Mestroni 2 and Orfeo Sbaizero 1,* 1 Department of Engineering and Architecture, University of Trieste, 34127 Trieste, Italy; [email protected] 2 University of Colorado Cardiovascular Institute, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA; [email protected] * Correspondence: [email protected]; Tel.: +39-040-5583770 Received: 15 July 2020; Accepted: 10 August 2020; Published: 15 August 2020 Abstract: Cardiomyopathies affect individuals worldwide, without regard to age, sex and ethnicity and are associated with significant morbidity and mortality. Inherited cardiomyopathies account for a relevant part of these conditions. Although progresses have been made over the years, early diagnosis and curative therapies are still challenging. Understanding the events occurring in normal and diseased cardiac cells is crucial, as they are important determinants of overall heart function. Besides chemical and molecular events, there are also structural and mechanical phenomena that require to be investigated. Cell structure and mechanics largely depend from the cytoskeleton, which is composed by filamentous proteins that can be cross-linked via accessory proteins. Alpha-actinin 2 (ACTN2), filamin C (FLNC) and dystrophin are three major actin cross-linkers that extensively contribute to the regulation of cell structure and mechanics. Hereby, we review the current understanding of the roles played by ACTN2, FLNC and dystrophin in the onset and progress of inherited cardiomyopathies. With our work, we aim to set the stage for new approaches to study the cardiomyopathies, which might reveal new therapeutic targets and broaden the panel of genes to be screened.
[Show full text]
9.4 | Intermediate Filaments
354 9.4 | Intermediate Filaments The second of the three major cytoskeletal Microtubule elements to be discussed was seen in the electron microscope as solid, unbranched Intermediate filaments with a diameter of 10–12 nm. They were named in- filament termediate filaments (or IFs ). To date, intermediate filaments have only been identified in animal cells. Intermediate fila- ments are strong, flexible, ropelike fibers that provide mechani- cal strength to cells that are subjected to physical stress, Gold-labeled including neurons, muscle cells, and the epithelial cells that line anti-plectin the body’s cavities. Unlike microfilaments and microtubules, antibodies IFs are a chemically heterogeneous group of structures that, in Plectin humans, are encoded by approximately 70 different genes. The polypeptide subunits of IFs can be divided into five major classes based on the type of cell in which they are found (Table 9.2) as well as biochemical, genetic, and immunologic criteria. Figure 9.41 Cytoskeletal elements are connected to one another by We will restrict the present discussion to classes I-IV, which are protein cross-bridges. Electron micrograph of a replica of a small por- found in the construction of cytoplasmic filaments, and con- tion of the cytoskeleton of a fibroblast after selective removal of actin sider type V IFs (the lamins), which are present as part of the filaments. Individual components have been digitally colorized to assist inner lining of the nuclear envelope, in Section 12.2. visualization. Intermediate filaments (blue) are seen to be connected to IFs radiate through the cytoplasm of a wide variety of an- microtubules (red) by long wispy cross-bridges consisting of the fibrous imal cells and are often interconnected to other cytoskeletal protein plectin (green).
[Show full text]
Plastin L (LCP1) (NM 002298) Human Tagged ORF Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC201670 Plastin L (LCP1) (NM_002298) Human Tagged ORF Clone Product data: Product Type: Expression Plasmids Product Name: Plastin L (LCP1) (NM_002298) Human Tagged ORF Clone Tag: Myc-DDK Symbol: LCP1 Synonyms: CP64; HEL-S-37; L-PLASTIN; LC64P; LPL; PLS2 Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 5 Plastin L (LCP1) (NM_002298) Human Tagged ORF Clone – RC201670 ORF Nucleotide >RC201670 ORF sequence Sequence: Red=Cloning site Blue=ORF Green=Tags(s) TTTTGTAATACGACTCACTATAGGGCGGCCGGGAATTCGTCGACTGGATCCGGTACCGAGGAGATCTGCC GCCGCGATCGCC ATGGCCAGAGGATCAGTGTCCGATGAGGAAATGATGGAGCTCAGAGAAGCTTTTGCCAAAGTTGATACTG ATGGCAATGGATACATCAGCTTCAATGAGTTGAATGACTTGTTCAAGGCTGCTTGCTTGCCTTTGCCTGG GTATAGAGTACGAGAAATTACAGAAAACCTGATGGCTACAGGTGATCTGGACCAAGATGGAAGGATCAGC TTTGATGAGTTTATCAAGATTTTCCATGGCCTAAAAAGCACAGATGTTGCCAAGACCTTTAGAAAAGCAA TCAATAAGAAGGAAGGGATTTGTGCAATCGGTGGTACTTCAGAGCAGTCTAGCGTTGGCACCCAACACTC CTATTCAGAGGAAGAAAAGTATGCCTTTGTCAACTGGATAAACAAAGCCCTGGAAAATGATCCTGATTGT CGGCATGTCATCCCAATGAACCCAAACACGAATGATCTCTTTAATGCTGTTGGAGATGGCATTGTCCTTT GTAAAATGATCAACCTGTCAGTGCCAGACACAATTGATGAAAGAACAATCAACAAAAAGAAGCTAACCCC
[Show full text]