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Book
Western blotting for the non-expert
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ISBN: 3030706842 3030706826 Year: 2021 Publisher: Cham, Switzerland : Springer,

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Book
Western blotting guru
Authors: ---
ISBN: 0128135387 0128135379 9780128135389 9780128135372 Year: 2017 Publisher: London, England : Academic Press,

Protein blotting : a practical approach.
Author:
ISBN: 0199634386 0199634378 9780199634378 Year: 1996 Volume: 140 Publisher: Oxford IRL press

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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.


Digital
Application of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics : A Replacement for Western Blot Analysis
Authors: ---
ISBN: 9781461486664 Year: 2013 Publisher: New York, NY Springer

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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.


Book
Principles of gene manipulation : an introduction to genetic engineering
Authors: ---
ISBN: 0632026081 9780632026081 Year: 1989 Volume: 2 Publisher: Oxford ; London ; Edinburgh... [et al.] : Blackwell Scientific Publications,

Molecular methods for virus detection
Authors: ---
ISBN: 0127489207 9786611054496 1281054496 0080536891 9780127489209 9780080536897 9781281054494 Year: 1995 Publisher: San Diego Academic Press

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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

Protein structure analysis : Preparation, characterization, and microsequencing.
Authors: --- ---
ISBN: 3540615008 3642477658 3642592198 Year: 1996 Publisher: Berlin : Springer,

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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.

Gene cloning and manipulation
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ISBN: 0521407001 0521403413 9780521407007 Year: 1995 Publisher: Cambridge ; New York, NY : Cambridge University Press,

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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.

Pharmaceutical biotechnology : an introduction for pharmacists and pharmaceutical scientists
Authors: ---
ISBN: 9057022494 Year: 1997 Publisher: Amsterdam Harwood


Book
Application of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics : A Replacement for Western Blot Analysis
Authors: ---
ISBN: 1461486653 1461486661 Year: 2013 Publisher: New York, NY : Springer New York : Imprint: Springer,

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Abstract

  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.

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