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Western immunoblotting --- Immunoblotting, Western --- Protein blotting --- Western blot analysis --- Western blotting --- Immunoblotting --- Proteins --- Analysis --- Immunologia --- Proteïnes
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Western immunoblotting --- Molecular biology. --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Immunoblotting, Western --- Protein blotting --- Western blot analysis --- Western blotting --- Immunoblotting --- Proteins --- Analysis
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Protein blotting techniques have become common laboratory procedures in the past few years. This text is written by scientists with expertise in these techniques. The versatility of the methods utilizing these procedures have brought about the development of different solid support matrices, as well as a wide variety of protein detection methods. While the most commonly used method in protein blotting is the use of antibodies to detect protein antigens, this technology has been expanded to examine a number of different interactions between proteins and other proteins, as well as other molecules such as carbohydrates and DNA. These methods have further been adapted for amino acid sequencing and purification of proteins for use as immunogens. This book outlines, in detail, numerous protocols and procedures which should help investigators design methods which will be optimal for their specific use.
Western immunoblotting --- Blotting, Western. --- Proteins --- 577.112 --- 57.088.1 --- 57.088.1 Methods for analysis and estimation --- Methods for analysis and estimation --- 577.112 Proteins --- Blot, Western --- Immunoblot, Western --- Western Blot --- Western Immunoblot --- Immunoblotting, Western --- Western Blotting --- Western Immunoblotting --- Blots, Western --- Blottings, Western --- Immunoblots, Western --- Immunoblottings, Western --- Western Blots --- Western Blottings --- Western Immunoblots --- Western Immunoblottings --- Protein blotting --- Western blot analysis --- Western blotting --- Immunoblotting --- Laboratory manuals. --- analysis. --- Analysis --- Blotting, Western --- Laboratory manuals --- analysis --- Analysis. --- Proteins - analysis --- Western immunoblotting - Laboratory manuals
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A key experiment in biomedical research is monitoring the expression of different proteins in order to detect changes that occur in biological systems under different experimental conditions. The method that is most widely used is the Western blot analysis. While Western blot is a workhorse in laboratories studying protein expression and has several advantages, it also has a number of significant limitations. In particular, the method is semi-quantitative with limited dynamic range. Western blot focuses on a single protein per sample with only a small number of representative samples analyzed in an experiment. New quantitative tools have been needed for some time to at least supplement, & possibly replace, the Western blot. Mass spectrometric methods have begun to compete with Western blot for routine quantitative analyses of proteins. One of these methods is based on the tandem mass spectrometry technique of selected reaction monitoring (SRM), which is also called multiple reaction monitoring (MRM). Selected reaction monitoring is actually an older tandem mass spectrometry technique, first described in the late 70s, that is widely utilized in the quantitative analysis of small molecules like drugs & metabolites. The use of selected reaction monitoring for the quantitative analysis of proteins has a number of advantages. Most importantly, it is fundamentally quantitative with a wide dynamic range. The output of the analysis is a numerical result that can range over several orders of magnitude. Other advantages include sufficient specificity & sensitivity to detect low abundance proteins in complex mixtures. Finally, selected reaction monitoring can be multiplexed to allow the quantitative analysis of relatively large numbers of proteins in a single sample in a single experiment. This Brief will explain both the theoretical & experimental details of the selected reaction monitoring experiment as it is applied to proteins.
Spectrometric and optical chemical analysis --- Genetics --- General biochemistry --- Human biochemistry --- Pathological biochemistry --- Human medicine --- massaspectrometrie --- western blotting --- medische biochemie --- proteomics --- biochemie --- biomedische wetenschappen --- moleculaire biologie --- proteïnen
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57.08 --- 577.21 --- biochemie --- biologie --- blotting --- gastheerorganismen --- genetica --- genetische manipulatie --- hybridisatie --- klonen --- laboratoriumbiochemie --- laboratoriumbiologie --- moleculaire biologie --- probes --- restrictie enzymen --- transformaties --- vectoren biologie --- biologische technieken, experimentele methoden en uitrusting in het algemeen --- Molecular biology --- antropogenetica --- Genetic engineering --- Génie génétique
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Molecular diagnostic procedures have been described in a number of recent books and articles. However, these publications have not focused on virus detection, nor have they provided practical protocols for the newer molecular methods.Written by the inventors or principal developers of these technologies, Molecular Methods for Virus Detection provides both reviews of individual methods and instructions for detecting virus nucleic acid sequences in clinical specimens. Each procedure includes quality assurance protocols that are often ignored by other methodology books. Molecular Me
Nucleic acid probes --- Polymerase chain reaction --- Virus diseases --- -Molecular diagnosis --- 57.083 --- 616-093 --- HIV human immunodeficiency virus --- NASBA --- PCR polymerase chain reaction --- biochemie --- biologie --- blotting --- chemiluminescentie --- diagnostiek --- geneeskunde --- hybridisatie --- kwaliteitscontrole --- laboratoriumbiologie --- ligase kettingreactie --- nucleïnezuren --- virusinfecties --- virussen --- Viral diseases --- Viral infections --- Virus infections --- Communicable diseases --- Medical virology --- Pathogenic viruses --- Chain reaction, Polymerase --- PCR (Biochemistry) --- Polymerization --- DNA polymerases --- Oligonucleotide probes --- Probes, Nucleic acid --- Molecular probes --- Molecular diagnosis --- Polymerase chain reaction. --- Nucleic acid probes. --- Molecular diagnosis. --- Virus diseases - - Molecular diagnosis
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The structure of a protein is essential for its function. Therefore, a variety of methods for analyzing protein structure have been developed recently; the most advanced and sensitive techniques have been selected for this manual. The presented procedures are well established and have been found useful in many laboratories; they are easy to perform and thus also suitable for beginners. Enclosed are protocols on the separation of proteins and peptides, manual and automated microsequencing, electrophoresis and blotting, analysis of amino acids, identification of cysteine residues and lipids as well as on mass spectrometry crystallization of macromolecules.
proteins --- peptides --- Chromatography --- genetic engineering --- Electrophoresis --- Amino acids --- Identification --- identification --- Spectrometry --- recombination --- Crystallization --- HPLC --- 543.64 --- 57.085 --- 612.08 --- massaspectrometrie --- sequentie-analyse --- Proteins --- Structure --- Laboratory manuals. --- identification. --- 57.088 --- aminozuren --- analytische chemie (scheikunde) --- biochemie --- biologie --- blotting --- elektroforese --- HPLC high performance liquid chromatography --- laboratoriumbiochemie --- peptiden --- proteïnen --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Structure&delete& --- Laboratory manuals --- Biochemistry. --- Cell biology. --- Biochemistry, general. --- Cell Biology. --- Cell biology --- Cellular biology --- Biology --- Cells --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition --- Macromolecule
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This text gives a broad, but concise, coverage of gene cloning and manipulation, suitable for undergraduates and beginning graduate students. Assuming only general biochemical knowledge, it stresses the concepts underlying particular types of cloning vector, and uses examples to illustrate them, rather than simply presenting a mass of detailed lists and vector maps. The book starts by describing the principles behind cloning DNA in E. coli, the enzymes used, the range of cloning vectors available, and how to screen libraries to find particular clones. The author shows how PCR can be used as an alternative, or complementary, approach. He then goes on to describe how sequences can be exploited, after cloning and identification, by site-directed mutagenesis and over-expression. The book finishes with a detailed presentation of the genetic manipulation of other organisms, including other bacteria, yeast, plants, insects, and mammals.
genetische engineering (manipulatie) --- kloneren (klonen) --- genetica (genen) --- génie génétique (ingénierie génétique) --- clonage --- génétique (gènes) --- PCR polymerase chain reaction --- bacteriofagen --- blotting --- clonen --- gastheerorganismen --- gelelektroforese --- laboratoriumbiologie --- plasmiden --- rDNA recombinant DNA --- restrictie enzymen --- vectoren biologie --- biologische technieken, experimentele methoden en uitrusting in het algemeen --- Molecular cloning --- 57.08 --- 577.21 --- biochemie --- biologie --- genetica --- genetische manipulatie --- modificatie --- moleculaire biologie --- mutagenen --- #ABIB:aimm --- Cloning, Molecular --- DNA cloning --- Gene cloning --- Cloning --- Genetic engineering --- Molecular genetics --- Clone cells --- Molecular cloning.
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biotechnologie --- Biotechnology --- pharmacology --- farmacologie --- Pharmacognosy --- Pharmacosynthesis. Pharmacochemistry --- Pharmacology. Therapy --- 57.08 --- 576.3 --- 579.6 --- 579.63 --- 579.66 --- ELISA enzyme linked immunosorbent assays --- PCR polymerase chain reaction --- absorptie --- antistoffen --- biochemie --- biochemische ingenieurstechnieken --- biofarmacie --- biologie --- blotting --- celfysiologie --- centrifugeren --- chromatografie --- downstream processing --- elektroforese --- farmacokinetica --- filtratie --- geneesmiddelen --- genen --- genetische manipulatie --- gentherapie --- hormonen --- hybridisatie --- immunoassays --- lever --- massaspectrometrie --- microbiologie --- moleculaire biologie --- mutagenese --- nieren --- procestechnologie --- proteïnen --- recombinant DNA --- sequentie-analyse --- transcriptie --- translatie --- vaccins --- voeding --- biologische technieken, experimentele methoden en uitrusting in het algemeen --- toegepaste microbiologie --- hygiënische microbiologie --- industriële en chemische microbiologie --- biogeneesmiddelen --- interferon --- vaccinatie
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A key experiment in biomedical research is monitoring the expression of different proteins in order to detect changes that occur in biological systems under different experimental conditions. The method that is most widely used is the Western blot analysis. While Western blot is a workhorse in laboratories studying protein expression and has several advantages, it also has a number of significant limitations. In particular, the method is semi-quantitative with limited dynamic range. Western blot focuses on a single protein per sample with only a small number of representative samples analyzed in an experiment. New quantitative tools have been needed for some time to at least supplement, & possibly replace, the Western blot. Mass spectrometric methods have begun to compete with Western blot for routine quantitative analyses of proteins. One of these methods is based on the tandem mass spectrometry technique of selected reaction monitoring (SRM), which is also called multiple reaction monitoring (MRM). Selected reaction monitoring is actually an older tandem mass spectrometry technique, first described in the late 70s, that is widely utilized in the quantitative analysis of small molecules like drugs & metabolites. The use of selected reaction monitoring for the quantitative analysis of proteins has a number of advantages. Most importantly, it is fundamentally quantitative with a wide dynamic range. The output of the analysis is a numerical result that can range over several orders of magnitude. Other advantages include sufficient specificity & sensitivity to detect low abundance proteins in complex mixtures. Finally, selected reaction monitoring can be multiplexed to allow the quantitative analysis of relatively large numbers of proteins in a single sample in a single experiment. This Brief will explain both the theoretical & experimental details of the selected reaction monitoring experiment as it is applied to proteins.
Biomedicine. --- Data mining. --- Proteins -- Analysis. --- Proteomics. --- Proteomics --- Proteins --- Amino Acids, Peptides, and Proteins --- Biochemistry --- Immunoblotting --- Immunoassay --- Biological Science Disciplines --- Chemicals and Drugs --- Immunologic Tests --- Natural Science Disciplines --- Disciplines and Occupations --- Laboratory Techniques and Procedures --- Diagnosis --- Analytical, Diagnostic and Therapeutic Techniques and Equipment --- Blotting, Western --- Analysis --- Analysis. --- Methodology. --- Medicine. --- Mass spectrometry. --- Biochemistry. --- Biomedicine general. --- Mass Spectrometry. --- Biochemistry, general. --- Molecular biology --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Mass spectra --- Mass spectrograph --- Mass spectroscopy --- Mass spectrum analysis --- Mass (Physics) --- Nuclear spectroscopy --- Spectrum analysis --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Composition --- Health Workforce --- Biomedicine, general.
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