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Titlebook: Affinity Chromatography; Methods and Protocol B. Vijayalakshmi Ayyar,Sushrut Arora Book 2022 Springer Science+Business Media, LLC, part of

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Robotic Affinity Purification of Soluble and Insoluble Recombinant Glutathione-S-Transferase Fusion usion bodies, is described. Depending on the expression levels and the amount of glutathione affinity matrix employed, the protocol yields approximately 30–100 μg of purified GST-fusion protein from 2 mL microplate cultures. The high yield is facilitated by employing an efficient chemical/enzymatic
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Application of Immunoaffinity Mass Spectrometry (IA-MS) for Protein Biomarker Quantificationralleled specificity. Typically, the protein antigen of interest is captured from biofluids and tissue lysates using an antibody prior to mass spectrometric analysis. Here we describe the specific steps of the protein immunoaffinity component of the IA-MS workflow that is applicable to most protein
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Arginine-Affinity Chromatography for Nucleic Acid (DNA and RNA) Isolation gene defects. In this context, biotechnology plays a critical role on establishing suitable processes for biopharmaceuticals manufacturing, while the purification step still imposes a major burden. Affinity chromatography using amino acids as specific ligands has been successfully applied for plasm
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Purification and Analysis of Nucleotides and Nucleosides from Plantson with liquid chromatography coupled to mass spectrometry enables the sensitive detection and quantification of metabolites of low abundance. Utilizing a liquid–liquid extraction in combination with a weak anion-exchange solid phase extraction enables the separation of negatively charged molecules
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Selection and Application of Aptamer Affinity for Protein Purificationd by using a reiterative in vitro selection procedure, named SELEX, in which the target is exposed to a combinatorial oligonucleotide combinatorial library. Target bound oligonucleotides are eluted, and PCR amplified followed by the next SELEX round. The process is repeated until no further increase
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Preparation of Affinity Chromatography Monolith in Miniaturized Format and Application for Protein S urine, etc.). Conventional chromatography resins possess technical limitations at mini-analytical scale, which was overcome with the use of alternative material known as monoliths. This chapter discusses on the how to modify the fused silica capillary inner surface, prepare polymer monoliths within
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Ligand Immobilization Methods for Affinity Chromatographyed for the numerous applications such as purification, scavenging, and target quantification. Therefore, it becomes critical to understand the chemical nature of these materials to select optimum conditions for ligand immobilization. In this chapter, we have explained some commonly employed ligand i
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