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Full-length myocilin (MYOC) protein is purified from mammalian cells as a dimer

Katoli, Parvaneh and Godbole, Adarsh and Romanowski, Michael and Clark, Kirk and Meredith, Erik and Saenz-Vash, Veronica and Wang, Yingqi and Lewicki, Nancy and Nguyen, Andrew and Lynch, Jeffrey (2018) Full-length myocilin (MYOC) protein is purified from mammalian cells as a dimer. Protein expression and purification, 147 (2018). pp. 38-48. ISSN 1096-0279; 1046-5928

Abstract

Myocilin (MYOC) is the gene with mutations most commonly observed in glaucoma patients. MYOC protein collected from patients and analyzed under non-reducing conditions suggests that MYOC is not normally found in a monomeric form. MYOC was first reported almost 20 years ago; however, a technical challenge still faced by researchers is an inability to isolate full-length MYOC protein for experimental purposes. Herein we describe two methods by which to isolate sufficient quantities of full-length MYOC protein from mammalian cells. Analytical size exclusion chromatography of isolated full-length MYOC protein indicated that it is predominantly dimeric and we propose a structure for the MYOC dimer. By sharing methods to obtain full-length MYOC protein, we hope to provide researchers with a tool that has previously not been available. The ultimate goal of MYOC research is to understand this target so we can help the patient that carries a MYOC mutation retain vision and maintain quality of life.

Item Type: Article
Date Deposited: 17 Nov 2018 00:45
Last Modified: 17 Nov 2018 00:45
URI: https://oak.novartis.com/id/eprint/34544

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