T611384 Anti-MAP4 Rabbit Pab

Total Page：16

File Type：pdf, Size：1020Kb

T611384 Anti-MAP4 Rabbit pAb Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL √ √ Web www.ab-mart.com.cn Product Information Description MAP4 rabbit polyclonal Protein full name Microtubule-associated protein 4 Synonyms MAP-4, Map4, Mtap4, DKFZp779A1753, MGC8617 Immunogen Recombinant protein corresponding to Mouse MAP4 Isotype IgG Purity Affinity purification Subcellular location Cytoplasm Uniprot ID P27816, P27546 Applications Applications IHC Species Human, Mouse Dilution 1: 1000-1: 2000 Positive Tissue lung cancer, colon cancer, ovary cancer, spleen, kidney Background The protein encoded by this gene is a major non-neuronal microtubule-associated protein. This protein contains a domain similar to the microtubule-binding domains of neuronal microtubule- associated protein (MAP2) and microtubule-associated protein tau (MAPT/TAU). This protein promotes microtubule assembly, and has been shown to counteract destabilization of interphase microtubule catastrophe promotion. Cyclin B was found to interact with this protein, which targets cell division cycle 2 (CDC2) kinase to microtubules. The phosphorylation of this protein affects microtubule properties and cell cycle progression. Images Immunohistochemistry analysis of paraffin-embedded human lung cancer using MAP4 (T611384M) at dilution of 1: 1900 Immunohistochemistry analysis of paraffin-embedded human colon cancer using MAP4 (T611384M) at dilution of 1: 1900 Immunohistochemistry analysis of paraffin-embedded human ovary cancer using MAP4 (T611384M) at dilution of 1: 1900 Immunohistochemistry analysis of paraffin-embedded human ovary cancer using MAP4 (T611384M) at dilution of 1: 1900 Immunohistochemistry analysis of paraffin-embedded mouse spleen using MAP4 (T611384M) at dilution of 1: 1900 Immunohistochemistry analysis of paraffin-embedded mouse kidney using MAP4 (T611384M) at dilution of 1: 1900 Storage Storage Store at -20 ℃ for one year. Avoid repeated freeze/ thaw cycles. Storage Buffer PBS with 0.02% sodium azide, 100 μg/ml BSA and 50% glycerol. NOTE: This product is intended for research only..

Copy Link

Recommended publications

Specialized Cilia in Mammalian Sensory Systems
Cells 2015, 4, 500-519; doi:10.3390/cells4030500 OPEN ACCESS cells ISSN 2073-4409 www.mdpi.com/journal/cells Review Specialized Cilia in Mammalian Sensory Systems Nathalie Falk, Marlene Lösl, Nadja Schröder and Andreas Gießl * Department of Biology, Animal Physiology, University of Erlangen-Nuremberg, 91058 Erlangen, Germany; E-Mails: [email protected] (N.F.); [email protected] (M.L.); [email protected] (A.G.) * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +49-9131-85-28055; Fax: +49-9131-85-28060. Academic Editors: Gang Dong and William Tsang Received: 18 May 2015 / Accepted: 9 September 2015 / Published: 11 September 2015 Abstract: Cilia and flagella are highly conserved and important microtubule-based organelles that project from the surface of eukaryotic cells and act as antennae to sense extracellular signals. Moreover, cilia have emerged as key players in numerous physiological, developmental, and sensory processes such as hearing, olfaction, and photoreception. Genetic defects in ciliary proteins responsible for cilia formation, maintenance, or function underlie a wide array of human diseases like deafness, anosmia, and retinal degeneration in sensory systems. Impairment of more than one sensory organ results in numerous syndromic ciliary disorders like the autosomal recessive genetic diseases Bardet-Biedl and Usher syndrome. Here we describe the structure and distinct functional roles of cilia in sensory organs like the inner ear, the olfactory epithelium, and the retina of the mouse. The spectrum of ciliary function in fundamental cellular processes highlights the importance of elucidating ciliopathy-related proteins in order to find novel potential therapies.
[Show full text]
Microtubule Organization and Microtubule- Associated Proteins (Maps)
Chapter 3 Microtubule Organization and Microtubule- Associated Proteins (MAPs) Elena Tortosa, Lukas C. Kapitein, and Casper C. Hoogenraad Abstract Dendrites have a unique microtubule organization. In vertebrates, den- dritic microtubules are organized in antiparallel bundles, oriented with their plus ends either pointing away or toward the soma. The mixed microtubule arrays control intracellular trafﬁcking and local signaling pathways, and are essential for dendrite development and function. The organization of microtubule arrays largely depends on the combined function of different microtubule regulatory factors or generally named microtubule-associated proteins (MAPs). Classical MAPs, also called structural MAPs, were identiﬁed more than 20 years ago based on their ability to bind to and copurify with microtubules. Most classical MAPs bind along the microtubule lattice and regulate microtubule polymerization, bundling, and stabilization. Recent evidences suggest that classical MAPs also guide motor protein transport, interact with the actin cytoskeleton, and act in various neuronal signaling networks. Here, we give an overview of microtubule organization in dendrites and the role of classical MAPs in dendrite development, dendritic spine formation, and synaptic plasticity. Keywords Neuron • Dendrite • Cytoskeleton • Microtubule • Microtubule- associated protein • MAP1 • MAP2 • MAP4 • MAP6 • MAP7 • MAP9 • Tau 3.1 Introduction Microtubules (MTs) are cytoskeletal structures that play essential roles in all eukaryotic cells. MTs are important not only during cell division but also in non-dividing cells, where they are critical structures in numerous cellular processes such as cell motility, migration, differentiation, intracellular transport and organelle positioning. MTs are composed of two proteins, α- and β-tubulin, that form heterodimers and organize themselves in a head-to-tail manner.
[Show full text]
"The Genecards Suite: from Gene Data Mining to Disease Genome Sequence Analyses". In: Current Protocols in Bioinformat
The GeneCards Suite: From Gene Data UNIT 1.30 Mining to Disease Genome Sequence Analyses Gil Stelzer,1,5 Naomi Rosen,1,5 Inbar Plaschkes,1,2 Shahar Zimmerman,1 Michal Twik,1 Simon Fishilevich,1 Tsippi Iny Stein,1 Ron Nudel,1 Iris Lieder,2 Yaron Mazor,2 Sergey Kaplan,2 Dvir Dahary,2,4 David Warshawsky,3 Yaron Guan-Golan,3 Asher Kohn,3 Noa Rappaport,1 Marilyn Safran,1 and Doron Lancet1,6 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel 2LifeMap Sciences Ltd., Tel Aviv, Israel 3LifeMap Sciences Inc., Marshﬁeld, Massachusetts 4Toldot Genetics Ltd., Hod Hasharon, Israel 5These authors contributed equally to the paper 6Corresponding author GeneCards, the human gene compendium, enables researchers to effectively navigate and inter-relate the wide universe of human genes, diseases, variants, proteins, cells, and biological pathways. Our recently launched Version 4 has a revamped infrastructure facilitating faster data updates, better-targeted data queries, and friendlier user experience. It also provides a stronger foundation for the GeneCards suite of companion databases and analysis tools. Improved data uniﬁcation includes gene-disease links via MalaCards and merged biological pathways via PathCards, as well as drug information and proteome expression. VarElect, another suite member, is a phenotype prioritizer for next-generation sequencing, leveraging the GeneCards and MalaCards knowledgebase. It au- tomatically infers direct and indirect scored associations between hundreds or even thousands of variant-containing genes and disease phenotype terms. Var- Elect’s capabilities, either independently or within TGex, our comprehensive variant analysis pipeline, help prepare for the challenge of clinical projects that involve thousands of exome/genome NGS analyses.
[Show full text]
Genetic Dissection of Intermated Recombinant Inbred Lines Using a New Genetic Map of Maize
Copyright Ó 2006 by the Genetics Society of America DOI: 10.1534/genetics.106.060376 Genetic Dissection of Intermated Recombinant Inbred Lines Using a New Genetic Map of Maize Yan Fu,*,1 Tsui-Jung Wen,† Yefim I. Ronin,‡ Hsin D. Chen,† Ling Guo,§ David I. Mester,‡ Yongjie Yang,* Michael Lee,† Abraham B. Korol,‡ Daniel A. Ashlock** and Patrick S. Schnable*,†,§,††,2 *Interdepartmental Genetics Graduate Program, Iowa State University, Ames, Iowa 50011, †Department of Agronomy, Iowa State University, Ames, Iowa 50011, ‡Institute of Evolution, University of Haifa, Haifa 31905, Israel, §Bioinformatics and Computational Biology Graduate Program, Iowa State University, Ames, Iowa 50011, **Department of Mathematics and Statistics, University of Guelph, Guelph, Ontario N1G 2W1, Canada and ††Center for Plant Genomics, Iowa State University, Ames, Iowa 50011-3467 Manuscript received July 6, 2006 Accepted for publication August 21, 2006 ABSTRACT A new genetic map of maize, ISU–IBM Map4, that integrates 2029 existing markers with 1329 new indel polymorphism (IDP) markers has been developed using intermated recombinant inbred lines (IRILs) from the intermated B73 3 Mo17 (IBM) population. The website http://magi.plantgenomics.iastate.edu pro- vides access to IDP primer sequences, sequences from which IDP primers were designed, optimized marker- specific PCR conditions, and polymorphism data for all IDP markers. This new gene-based genetic map will facilitate a wide variety of genetic and genomic research projects, including map-based genome sequencing and gene cloning. The mosaic structures of the genomes of 91 IRILs, an important resource for identifying and mapping QTL and eQTL, were defined. Analyses of segregation data associated with markers genotyped in three B73/Mo17-derived mapping populations (F2, Syn5, and IBM) demonstrate that allele frequencies were significantly altered during the development of the IBM IRILs.
[Show full text]
The MAP2/Tau Family of Microtubule-Associated Proteins Comment Leif Dehmelt and Shelley Halpain
Protein family review The MAP2/Tau family of microtubule-associated proteins comment Leif Dehmelt and Shelley Halpain Address: Department of Cell Biology, The Scripps Research Institute and Institute for Childhood and Neglected Diseases, 10550 North Torrey Pines Rd, La Jolla, CA 92037, USA. Correspondence: Shelley Halpain. E-mail: [email protected] reviews Published: 23 December 2004 Genome Biology 2004, 6:204 The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2004/6/1/204 © 2004 BioMed Central Ltd reports Summary Microtubule-associated proteins (MAPs) of the MAP2/Tau family include the vertebrate proteins MAP2, MAP4, and Tau and homologs in other animals. All three vertebrate members of the family have alternative splice forms; all isoforms share a conserved carboxy-terminal domain containing microtubule-binding repeats, and an amino-terminal projection domain of varying size. deposited research MAP2 and Tau are found in neurons, whereas MAP4 is present in many other tissues but is generally absent from neurons. Members of the family are best known for their microtubule- stabilizing activity and for proposed roles regulating microtubule networks in the axons and dendrites of neurons. Contrary to this simple, traditional view, accumulating evidence suggests a much broader range of functions, such as binding to filamentous (F) actin, recruitment of signaling proteins, and regulation of microtubule-mediated transport. Tau is also implicated in Alzheimer’s disease and other dementias. The ability of MAP2 to interact with both microtubules and F-actin might be critical for neuromorphogenic processes, such as neurite initiation, during which refereed research networks of microtubules and F-actin are reorganized in a coordinated manner.
[Show full text]
Transposon Mutagenesis Identifies Genetic Drivers of Brafv600e Melanoma
ARTICLES Transposon mutagenesis identifies genetic drivers of BrafV600E melanoma Michael B Mann1,2, Michael A Black3, Devin J Jones1, Jerrold M Ward2,12, Christopher Chin Kuan Yew2,12, Justin Y Newberg1, Adam J Dupuy4, Alistair G Rust5,12, Marcus W Bosenberg6,7, Martin McMahon8,9, Cristin G Print10,11, Neal G Copeland1,2,13 & Nancy A Jenkins1,2,13 Although nearly half of human melanomas harbor oncogenic BRAFV600E mutations, the genetic events that cooperate with these mutations to drive melanogenesis are still largely unknown. Here we show that Sleeping Beauty (SB) transposon-mediated mutagenesis drives melanoma progression in BrafV600E mutant mice and identify 1,232 recurrently mutated candidate cancer genes (CCGs) from 70 SB-driven melanomas. CCGs are enriched in Wnt, PI3K, MAPK and netrin signaling pathway components and are more highly connected to one another than predicted by chance, indicating that SB targets cooperative genetic networks in melanoma. Human orthologs of >500 CCGs are enriched for mutations in human melanoma or showed statistically significant clinical associations between RNA abundance and survival of patients with metastatic melanoma. We also functionally validate CEP350 as a new tumor-suppressor gene in human melanoma. SB mutagenesis has thus helped to catalog the cooperative molecular mechanisms driving BRAFV600E melanoma and discover new genes with potential clinical importance in human melanoma. Substantial sun exposure and numerous genetic factors, including including BrafV600E, recapitulate the genetic and histological hallmarks skin type and family history, are the most important melanoma risk of human melanoma. In these models, increased MEK-ERK signaling factors. Familial melanoma, which accounts for <10% of cases, is asso- initiates clonal expansion of melanocytes, which is limited by oncogene- ciated with mutations in CDKN2A1, MITF2 and POT1 (refs.
[Show full text]
Table S1. 103 Ferroptosis-Related Genes Retrieved from the Genecards
Table S1. 103 ferroptosis-related genes retrieved from the GeneCards. Gene Symbol Description Category GPX4 Glutathione Peroxidase 4 Protein Coding AIFM2 Apoptosis Inducing Factor Mitochondria Associated 2 Protein Coding TP53 Tumor Protein P53 Protein Coding ACSL4 Acyl-CoA Synthetase Long Chain Family Member 4 Protein Coding SLC7A11 Solute Carrier Family 7 Member 11 Protein Coding VDAC2 Voltage Dependent Anion Channel 2 Protein Coding VDAC3 Voltage Dependent Anion Channel 3 Protein Coding ATG5 Autophagy Related 5 Protein Coding ATG7 Autophagy Related 7 Protein Coding NCOA4 Nuclear Receptor Coactivator 4 Protein Coding HMOX1 Heme Oxygenase 1 Protein Coding SLC3A2 Solute Carrier Family 3 Member 2 Protein Coding ALOX15 Arachidonate 15-Lipoxygenase Protein Coding BECN1 Beclin 1 Protein Coding PRKAA1 Protein Kinase AMP-Activated Catalytic Subunit Alpha 1 Protein Coding SAT1 Spermidine/Spermine N1-Acetyltransferase 1 Protein Coding NF2 Neurofibromin 2 Protein Coding YAP1 Yes1 Associated Transcriptional Regulator Protein Coding FTH1 Ferritin Heavy Chain 1 Protein Coding TF Transferrin Protein Coding TFRC Transferrin Receptor Protein Coding FTL Ferritin Light Chain Protein Coding CYBB Cytochrome B-245 Beta Chain Protein Coding GSS Glutathione Synthetase Protein Coding CP Ceruloplasmin Protein Coding PRNP Prion Protein Protein Coding SLC11A2 Solute Carrier Family 11 Member 2 Protein Coding SLC40A1 Solute Carrier Family 40 Member 1 Protein Coding STEAP3 STEAP3 Metalloreductase Protein Coding ACSL1 Acyl-CoA Synthetase Long Chain Family Member 1 Protein
[Show full text]
Genomic Variants Within Chromosome 14Q32.32 Regulate Bone Mass Through MARK3 Signaling in Osteoblasts
Genomic variants within chromosome 14q32.32 regulate bone mass through MARK3 signaling in osteoblasts Qian Zhang, … , Charles R. Farber, Thomas L. Clemens J Clin Invest. 2021;131(7):e142580. https://doi.org/10.1172/JCI142580. Research Article Bone Biology Bone mineral density (BMD) is a highly heritable predictor of osteoporotic fracture. GWAS have identified hundreds of loci influencing BMD, but few have been functionally analyzed. In this study, we show that SNPs within a BMD locus on chromosome 14q32.32 alter splicing and expression of PAR-1a/microtubule affinity regulating kinase 3 (MARK3), a conserved serine/threonine kinase known to regulate bioenergetics, cell division, and polarity. Mice lacking Mark3 either globally or selectively in osteoblasts have increased bone mass at maturity. RNA profiling from Mark3-deficient osteoblasts suggested changes in the expression of components of the Notch signaling pathway. Mark3-deficient osteoblasts exhibited greater matrix mineralization compared with controls that was accompanied by reduced Jag1/Hes1 expression and diminished downstream JNK signaling. Overexpression of Jag1 in Mark3-deficient osteoblasts both in vitro and in vivo normalized mineralization capacity and bone mass, respectively. Together, these findings reveal a mechanism whereby genetically regulated alterations in Mark3 expression perturb cell signaling in osteoblasts to influence bone mass. Find the latest version: https://jci.me/142580/pdf The Journal of Clinical Investigation RESEARCH ARTICLE Genomic variants within chromosome 14q32.32 regulate bone mass through MARK3 signaling in osteoblasts Qian Zhang,1,2 Larry D. Mesner,3 Gina M. Calabrese,3 Naomi Dirckx,1 Zhu Li,1,2 Angela Verardo,1 Qian Yang,1 Robert J.
[Show full text]
The Microtubule Skeleton and the Evolution of Neuronal Complexity in Vertebrates
Biol. Chem. 2019; 400(9): 1163–1179 Nataliya I. Trushina, Armen Y. Mulkidjanian and Roland Brandt* The microtubule skeleton and the evolution of neuronal complexity in vertebrates https://doi.org/10.1515/hsz-2019-0149 Received February 4, 2019; accepted April 17, 2019; previously Introduction published online May 22, 2019 The complexity of the nervous system permits the devel- Abstract: The evolution of a highly developed nervous opment of sophisticated behavioral repertoires, such as system is mirrored by the ability of individual neurons to language, tool use, self-awareness, symbolic thought, develop increased morphological complexity. As microtu- cultural learning and consciousness. The basis for the bules (MTs) are crucially involved in neuronal development, development of such a complexity is a high neuronal het- we tested the hypothesis that the evolution of complexity is erogeneity caused by neuronal diversification on the one driven by an increasing capacity of the MT system for regu- hand and a large interconnectivity between the individual lated molecular interactions as it may be implemented by neurons on the other hand (Muotri and Gage, 2006). In a higher number of molecular players and a greater ability addition, the brain constantly needs to adapt to func- of the individual molecules to interact. We performed bio- tional challenges of various kinds during development informatics analysis on different classes of components of and adulthood by a process called neural plasticity (Zilles, the vertebrate neuronal MT cytoskeleton. We show that the 1992). At a single cell level, neural plasticity involves number of orthologs of tubulin structure proteins, MT-bind- changes in the number or the strength of synaptic con- ing proteins and tubulin-sequestering proteins expanded tacts between individual neurons thereby changing the during vertebrate evolution.
[Show full text]
An Evolutionary Roadmap to the Microtubule-Associated Protein MAP Tau Frederik Sündermann1, Maria-Pilar Fernandez2 and Reginald O
Sündermann et al. BMC Genomics (2016) 17:264 DOI 10.1186/s12864-016-2590-9 RESEARCH ARTICLE Open Access An evolutionary roadmap to the microtubule-associated protein MAP Tau Frederik Sündermann1, Maria-Pilar Fernandez2 and Reginald O. Morgan2* Abstract Background: The microtubule associated protein Tau (MAPT) promotes assembly and interaction of microtubules with the cytoskeleton, impinging on axonal transport and synaptic plasticity. Its neuronal expression and intrinsic disorder implicate it in some 30 tauopathies such as Alzheimer’s disease and frontotemporal dementia. These pathophysiological studies have yet to be complemented by computational analyses of its molecular evolution and structural models of all its functional domains to explain the molecular basis for its conservation profile, its site-specific interactions and the propensity to conformational disorder and aggregate formation. Results: We systematically annotated public sequence data to reconstruct unspliced MAPT, MAP2 and MAP4 transcripts spanning all represented genomes. Bayesian and maximum likelihood phylogenetic analyses, genetic linkage maps and domain architectures distinguished a nonvertebrate outgroup from the emergence of MAP4 and its subsequent ancestral duplication to MAP2 and MAPT. These events were coupled to other linked genes such as KANSL1L and KANSL and may thus be consequent to large-scale chromosomal duplications originating in the extant vertebrate genomes of hagfish and lamprey. Profile hidden Markov models (pHMMs), clustered subalignments and 3D structural predictions defined potential interaction motifs and specificity determining sites to reveal distinct signatures between the four homologous microtubule binding domains and independent divergence of the amino terminus. Conclusion: These analyses clarified ambiguities of MAPT nomenclature, defined the order, timing and pattern of its molecular evolution and identified key residues and motifs relevant to its protein interaction properties and pathogenic role.
[Show full text]
1 Genetic Dissection of Intermated Recombinant Inbred Lines Using A
Genetics: Published Articles Ahead of Print, published on September 1, 2006 as 10.1534/genetics.106.060376 1 Genetic dissection of intermated recombinant inbred lines using a new genetic map of maize that includes 1,329 novel PCR-based genic markers Yan Fu*2, Tsui-Jung Wen†, Yefim I. Ronin‡, Hsin D. Chen†, Ling Guo§, David I. Mester‡, Yongjie Yang*, Michael Lee†, Abraham B. Korol‡, Daniel A. Ashlock¶, Patrick S. Schnable*†§||,1 *Interdepartmental Genetics Graduate Program, Iowa State University, Ames, IA 50011, USA †Department of Agronomy, Iowa State University, Ames, IA 50011, USA ‡Institute of Evolution, University of Haifa, Haifa 31905, Israel §Bioinformatics and Computational Biology Graduate Program, Iowa State University, Ames, IA 50011, USA ¶Department of Mathematics and Statistics, University of Guelph, ON Canada N1G 2W1 ||Center for Plant Genomics, Iowa State University, Ames, IA 50011-3467, USA 1Corresponding author 2Present address: Donald Danforth Plant Science Center, St. Louis, MO 63132 Sequence data from this article have been deposited with the EMBL/GenBank Data Libraries under accession nos. DQ207642~DQ207725. 2 Running Head Title: Maize genetic map and IRILs Key words: genetic map, recombinant inbred lines, gametic disequilibrium, QTL mapping, segregation distortion To whom correspondence should be addressed: Patrick S. Schnable, 2035B Roy J. Carver Co-Laboratory, Iowa State University, Ames, IA 50011-3650, USA Voice: 515-294-0975 Fax: 515-294-5256 E-mail: [email protected] 3 ABSTRACT A new genetic map of maize, ISU-IBM Map4, that integrates 2,029 existing markers with 1,329 new InDel Polymorphism (IDP) markers has been developed using Intermated Recombinant Inbred Lines (IRILs) from the Intermated B73xMo17 (IBM) population.
[Show full text]
Mouse Map4 Knockout Project (CRISPR/Cas9)
https://www.alphaknockout.com Mouse Map4 Knockout Project (CRISPR/Cas9) Objective: To create a Map4 knockout Mouse model (C57BL/6N) by CRISPR/Cas-mediated genome engineering. Strategy summary: The Map4 gene (NCBI Reference Sequence: NM_001205330 ; Ensembl: ENSMUSG00000032479 ) is located on Mouse chromosome 9. 19 exons are identified, with the ATG start codon in exon 2 and the TAA stop codon in exon 19 (Transcript: ENSMUST00000035055). Exon 4~13 will be selected as target site. Cas9 and gRNA will be co-injected into fertilized eggs for KO Mouse production. The pups will be genotyped by PCR followed by sequencing analysis. Note: Mice homozygous for a gene trapped allele are viable and do not display any overt phenotypic abnormalities. Exon 4 starts from about 8.68% of the coding region. Exon 4~13 covers 73.66% of the coding region. The size of effective KO region: ~42885 bp. The KO region does not have any other known gene. Page 1 of 10 https://www.alphaknockout.com Overview of the Targeting Strategy Wildtype allele 5' gRNA region gRNA region 3' 12 1 4 5 6 7 8 9 10 11 13 19 Legends Exon of mouse Map4 Knockout region Page 2 of 10 https://www.alphaknockout.com Overview of the Dot Plot (up) Window size: 15 bp Forward Reverse Complement Sequence 12 Note: The 2000 bp section upstream of Exon 4 is aligned with itself to determine if there are tandem repeats. Tandem repeats are found in the dot plot matrix. The gRNA site is selected outside of these tandem repeats. Overview of the Dot Plot (down) Window size: 15 bp Forward Reverse Complement Sequence 12 Note: The 2000 bp section downstream of Exon 13 is aligned with itself to determine if there are tandem repeats.
[Show full text]