id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-260869-rym2ik0o	Lemmermeyer, Tanja	Characterization of monoclonal antibodies against feline coronavirus accessory protein 7b	2016-02-29		.txt	text/plain	6482	389	58	The 7b protein has a molecular mass of $26 kDa, it is secreted from the cell and contains (i) a Cterminal KDEL-like endoplasmic reticulum (ER) retention signal, (ii) an N-terminal signal sequence of 17 amino acids and (iii) a potential N-glycosylation site at aa position 68 (Vennema et al., 1992a) . The identity of the purified protein was confirmed by SDS-PAGE and Western blotting using anti-His mAb. The protein had an apparent molecular mass of 24 kDa as judged by SDS-PAGE analysis, which is predicted for this protein, and was recognized by the His-tag-specific antibody (Fig. 1a) . Two additional minor bands in the SDS-PAGE were specifically recognized by Western blotting using the His-tag-specific mAb. These bands are consistent with a dimer and a 37-kDa degradation product, respectively, of the GST-7bDSS-His protein (Fig. 1b) . The results outlined above show that the anti-7b mAbs recognize exclusively the nonglycosylated form of the viral protein in FCoV-infected cells.	./cache/cord-260869-rym2ik0o.txt	./txt/cord-260869-rym2ik0o.txt