FUS (FUsed in Sarcoma), also known as TLS (Translocated in LipoSarcoma), is a multifunctional RNA/DNA-binding protein involved in transcriptional regulation, RNA splicing, transport, and translation. It plays critical roles in maintaining RNA homeostasis and stress granule dynamics. Antibodies targeting FUS/TLS are essential tools in studying its physiological functions and pathological implications.
Mutations in the *FUS* gene are linked to neurodegenerative diseases, notably amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). These mutations often cause cytoplasmic mislocalization of FUS, leading to toxic aggregates—a hallmark of disease pathology. FUS/TLS antibodies enable researchers to detect these aggregates, analyze subcellular distribution, and investigate disease mechanisms.
In cancer, chromosomal translocations involving *FUS* (e.g., FUS-DDIT3 in myxoid liposarcoma) generate oncogenic fusion proteins. Specific antibodies help identify these fusion products in diagnostic assays and explore their role in tumorigenesis. Additionally, FUS/TLS antibodies are used in techniques like immunoprecipitation, Western blotting, and immunohistochemistry to study protein interactions, post-translational modifications, and tissue-specific expression patterns.
Research using these antibodies has also revealed FUS’s involvement in DNA repair and phase separation processes. Their application continues to advance understanding of FUS-related pathways in both normal cellular function and disease, offering potential biomarkers or therapeutic targets for ALS, FTD, and cancers.