Amyloid Proteins

ยท Methods in molecular biology แƒฌแƒ˜แƒ’แƒœแƒ˜ 299 ยท Springer Science & Business Media
แƒ”แƒšแƒฌแƒ˜แƒ’แƒœแƒ˜
408
แƒ’แƒ•แƒ”แƒ แƒ“แƒ˜
แƒ แƒ”แƒ˜แƒขแƒ˜แƒœแƒ’แƒ”แƒ‘แƒ˜ แƒ“แƒ แƒ›แƒ˜แƒ›แƒแƒฎแƒ˜แƒšแƒ•แƒ”แƒ‘แƒ˜ แƒ“แƒแƒฃแƒ“แƒแƒกแƒขแƒฃแƒ แƒ”แƒ‘แƒ”แƒšแƒ˜แƒ ย แƒจแƒ”แƒ˜แƒขแƒงแƒ•แƒ”แƒ— แƒ›แƒ”แƒขแƒ˜

แƒแƒ› แƒ”แƒšแƒฌแƒ˜แƒ’แƒœแƒ˜แƒก แƒจแƒ”แƒกแƒแƒฎแƒ”แƒ‘

A proven collection of readily reproducible techniques for studying amyloid proteins and their involvement in the etiology, pathogenesis, diagnosis, and therapy of amyloid diseases. The contributors provide methods for the preparation of amyloid and its precursors (oligomers and protofibrils), in vitro assays and analytical techniques for their study, and cell culture models and assays for the production of amyloid proteins. Additional chapters present readily reproducible techniques for amyloid extraction from tissue, its detection in vitro and in vivo, as well as nontransgenic methods for developing amyloid mouse models. The protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.

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