id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-280679-jj3wzojy	Marblestone, Jeffrey G.	Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO	2006-01-01		.txt	text/plain	4854	250	54	For this study, three model proteins, enhanced green florescent protein (eGFP), matrix metalloprotease-13 (MMP13), and myostatin (growth differentiating factor-8, GDF8), were fused to the C termini of maltose-binding protein (MBP), glutathione S-transferase (GST), thioredoxin (TRX), NUS A, ubiquitin (Ub), and SUMO tags. Taken together, these results demonstrate that SUMO is superior to commonly used fusion tags in enhancing expression and solubility with the distinction of generating recombinant protein with native sequences. Three candidate proteins, enhanced green fluorescent protein (eGFP), and two previously described difficult-to-express proteins, matrix metalloprotease-13 (MMP13) and myostatin (growth differentiating factor-8, GDF8), were expressed as fusions with maltose-binding protein (MBP), glutathione S-transferase (GST), thioredoxin (TRX), NUS A, ubiquitin (Ub), and SUMO. The ability of commonly used fusion tags to enhance protein expression and solubility was investigated using three candidate proteins (eGFP, MMP13, and GDF8) and six fusion tags (SUMO, Ub, MBP, GST, TRX, and NUS A).	./cache/cord-280679-jj3wzojy.txt	./txt/cord-280679-jj3wzojy.txt