Ligand Affinity Chromatography, an Indispensable Method for the Purification of Soluble Cytokine Receptors and Binding Proteins
Ligand affinity chromatography separation is based on unique interaction between the target analyte and a ligand, which is coupled covalently to a resin. It is a simple, rapid, selective, and efficient purification procedure of proteins providing tens of thousands fold purification in one step. The biological activity of the isolated proteins is retained in most cases thus function is revealed concomitantly with the isolation. Prior to the completion of the genome project this method facilitated rapid and reliable cloning of the corresponding gene. Upon completion of this project, a partial protein sequence is enough for retrieving its complete mRNA and hence its complete protein sequence. This method is indispensable for the isolation of both expected (e.g. receptors) but mainly unexpected, unpredicted and very much surprising binding proteins. No other approach would yield the latter. This chapter provides examples for both the expected target proteins, isolated from rich sources of human proteins, as well as the unexpected binding proteins, found by serendipity.
- Transmembrane Signaling by G Protein-Coupled Receptors
- Isolation and Culture of Human Alveolar Epithelial Cells
- Gene Mapping to Chromosomes by Hybridization in Situ
- Quantitative Polymerase Chain Reaction
- A Human Cell Extract-Based Assay for the Activation of ATM and ATR Checkpoint Kinases
- Dissecting Nucleases into Their Structural and Functional Domains: Mapping the RNA-Binding Surface of RNase III by NMR
- Purification of Murine Monoclonal Antibodies
- Multiphoton Intravital Microscopy to Study Lymphocyte Motility in Lymph Nodes
- Cell子刊:科学家新研发一种技术快速将iPSC转化成为老化神经细胞
- 人类X染色质的观察