Purification of Amyloidogenic Transthyretin Protein Using NuviaQ Anion Exchange Resin

Sébastien Penninckx; Vincent Raussens; Stéphanie Deroo

Purification of Amyloidogenic Transthyretin Protein Using NuviaQ Anion Exchange Resin

Sébastien Penninckx
, Vincent Raussens (Supervisor)
, Stéphanie Deroo (Supervisor)

Research output: Contribution to journal › Article

Abstract

Purification of recombinant amyloidogenic proteins can sometimes prove challenging due in part to their aggregation-prone character, which prevent the use of acidic buffers or denaturant agents. Here, we demonstrate how we are able to use Bio-Rad's NuviaQ Resin to successfully purify one such protein, transthyretin, under neutral buffer conditions.

Original language	English
Journal	Bio-Rad Bulletin
Volume	6711
Publication status	Published - 2015
Externally published	Yes

Cite this

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title = "Purification of Amyloidogenic Transthyretin Protein Using NuviaQ Anion Exchange Resin",

abstract = "Purification of recombinant amyloidogenic proteins can sometimes prove challenging due in part to their aggregation-prone character, which prevent the use of acidic buffers or denaturant agents. Here, we demonstrate how we are able to use Bio-Rad's NuviaQ Resin to successfully purify one such protein, transthyretin, under neutral buffer conditions.",

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year = "2015",

language = "English",

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journal = "Bio-Rad Bulletin",

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T1 - Purification of Amyloidogenic Transthyretin Protein Using NuviaQ Anion Exchange Resin

AU - Penninckx, Sébastien

A2 - Raussens, Vincent

A2 - Deroo, Stéphanie

PY - 2015

Y1 - 2015

N2 - Purification of recombinant amyloidogenic proteins can sometimes prove challenging due in part to their aggregation-prone character, which prevent the use of acidic buffers or denaturant agents. Here, we demonstrate how we are able to use Bio-Rad's NuviaQ Resin to successfully purify one such protein, transthyretin, under neutral buffer conditions.

AB - Purification of recombinant amyloidogenic proteins can sometimes prove challenging due in part to their aggregation-prone character, which prevent the use of acidic buffers or denaturant agents. Here, we demonstrate how we are able to use Bio-Rad's NuviaQ Resin to successfully purify one such protein, transthyretin, under neutral buffer conditions.

M3 - Article

VL - 6711

JO - Bio-Rad Bulletin

JF - Bio-Rad Bulletin

ER -