{'fraction_non_alphanumeric': 0.02355072463768116, 'fraction_numerical': 0.02717391304347826, 'mean_word_length': 4.338164251207729, '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}}
A low content of ERCC1 and a 120 kDa protein is a frequent feature of group F xeroderma pigmentosum fibroblast cells.

The ERCC1 protein has been predicted to form part of a tight complex with a protein partner, the yet-unidentified XPF/ERCC4 protein, in normal human cells. We used an anti-ERCC1 antibody to detect the complex by immunoprecipitation and immunoblotting. The amount of ERCC1 protein expressed in five different XP-F cell strains was 1/ 5-1/34 of that of the protein in normal and XP cell strains representing other complementation groups. A 120 kDa protein was co-immunoprecipitated with ERCC1 by the anti-ERCC1 antibody, and the amount of the 120 kDa protein in XP-F cell strains was 1/5-1/8 of that of the protein in normal and XP cell strains representing other complementation groups. The XPA protein was not co-immunoprecipitated with ERCC1 in any cell strain. These results demonstrate that a low level of ERCC1 and the 120 kDa protein is a frequent feature of XP-F cell extracts and that a lower amount of a complex between these proteins occurs in XP-F cells than in normal cells.