{'fraction_non_alphanumeric': 0.04282868525896414, 'fraction_numerical': 0.013944223107569721, 'mean_word_length': 7.104838709677419, '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': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Immunohistochemical staining properties of amyloids with anti‐keratin antibodies using formalin‐fixed, paraffin‐embedded sections

Immunohistochemical staining properties of amyloids with anti‐keratin antibodies were investigated using an avidin‐biotin‐per‐oxidase complex (ABC) system on formalin‐fixed, paraffin‐embedded sections. Anti‐keratin antibody EAB‐903 which recognize 66K and 57K daltons keratin peptides reacted with amyloid deposits in both lichen amyloidosus (LA) and macular amyloidosis (MA), but did not react with either primary systemic amyloidosis (AL), secondary systemic amyloidosis (AA) or heredo‐familial amyloid polyneuropathy (AF). However, anti‐keratin antibodies EAB‐904 and MAK‐6 did not react with any types of amyloids. These results suggested that immunohistochemical staining with anti‐keratin antibody EAB‐903 using formalin‐fixed, paraffin‐embedded sections appeared to be a useful method in making differential diagnosis of primary localized cutaneous amyloidosis (AD).