{'fraction_non_alphanumeric': 0.043824701195219126, 'fraction_numerical': 0.045816733067729085, 'mean_word_length': 4.52014652014652, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 1, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Development of isoform-specific monoclonal antibodies against human IL-18 binding protein.

Interleukin-18 binding protein (IL-18BP) is a soluble antagonist of IL-18 originally discovered while attempting to isolate a soluble receptor by using IL-18-ligand affinity column. IL-18BP has four isoforms (a, b, c, and d) in humans and two isoforms (c and d) in mice. The human isoforms IL-18BPa and IL-18BPc neutralize IL-18 activity sufficiently at an equimolar ratio; however IL-18BPb and IL-18BPd isoforms lack a complete Ig domain at C-terminus and lose the ability to neutralize IL-18 activity. Mouse IL-18BPc and IL-18BPd isoforms, possessing a similar complete Ig domain, also neutralize the biological activity of mouse IL-18 at an equimolar ratio. Here we expressed recombinant proteins of the active human IL-18BP isoforms and developed monoclonal antibodies (MAbs) against human IL-18BP a and c isoforms. We obtained two MAbs (78-4 and 38-3) of human IL-18BPa and two MAbs (18-7 and 29-6) of human IL-18BPc. The MAb clones 18-7 and 29-6 specifically recognized recombinant IL-18BPc in Western blot analyses and ELISA, whereas the MAb clone 78-4 recognized both isoforms in Western blot analyses, but only human IL-18BPa isoform in ELISA. We developed a sandwich ELISA by using the monoclonal antibody specific to human IL-18BPa isoform. The isoform-specific anti-human IL-18BP MAb may be a useful tool in categorizing a distinct group of patients from various autoimmune diseases related to IL-18BP.