id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-000984-64p3wpav	Huang, Shang-Hui	Self-Oligomerization Is Essential for Enhanced Immunological Activities of Soluble Recombinant Calreticulin	2013-06-10		.txt	text/plain	5252	291	54	We herein further demonstrate that rCRT fragments 18–412 (rCRT/18-412), rCRT/39-272, rCRT/120-308 and rCRT/120-250 can self-oligomerize in solution and are 50–100 fold more potent than native CRT (nCRT, isolated from mouse livers) in activating macrophages in vitro. Additionally, rCRT/39-272, a prokaryotically-expressed murine CRT fragment covering amino acid residues 39-272 fused with an N-terminal His-tag, was extraordinarily potent in activating B cells and macrophages in vitro and also in eliciting specific Ab production in mice [16] . The sequence of rCRT/39-272 encompasses most of the globular N domain (aa residues , and we have previously shown that it possess lectin-like activity (selective binding with polysaccharides including carrageenan, alginic acids, and hyaluronic acids in ELISAs) [16] , implying that the prokaryotically expressed recombinant polypeptide retained the lectin activity of CRT. Purified nCRT, but not BSA or recombinant enhanced green fluorescence protein (rEGFP, 28 kDa with a His-tag), was positively recognized by CRT-Abs. As evidenced by native PAGE analysis, a substantial amount of rCRT/18-412 formed higher-molecular-weight oligomers, whilst nCRT existed mostly in monomeric form (Figs.	./cache/cord-000984-64p3wpav.txt	./txt/cord-000984-64p3wpav.txt