FUBP1 Antibody

The Far Upstream Element Binding Protein 1 (FUBP1), also known as human DNA helicase V (HDH V), is a multifunctional protein that plays a crucial role in the regulation of gene expression. It was first identified as a DNA-binding protein that regulates the transcription of the proto-oncogene c-Myc by binding to the far upstream element (FUSE) in the promoter region .

FUBP1 was discovered in 1994 when researchers identified its specific binding to the FUSE sequence, located approximately 1.5 kilobases upstream of the transcription start site of the c-Myc gene . The c-Myc gene is a critical regulator of cell proliferation, differentiation, and apoptosis, and its expression is tightly controlled by various transcription factors, including FUBP1 .

FUBP1 functions as a single-stranded DNA-binding protein that regulates the expression of target genes by binding to the FUSE in their upstream noncoding sequences . It collaborates with other transcription factors, such as TFIIH, to ensure optimal transcription of the c-Myc gene . In addition to its role in transcription, FUBP1 has been found to act as an RNA-binding protein, regulating the translation or stability of several mRNA species .

FUBP1 has been implicated in various cancers, including hepatocellular carcinoma (HCC) and other malignancies . Overexpression of FUBP1 promotes cancer cell proliferation, invasion, and metastasis by activating signaling pathways such as the transforming growth factor-β (TGF-β)/Smad pathway . Aberrant expression of FUBP1, mutations in the FUBP1 gene, or alternative splicing of its repressor FIR have been found in a variety of malignant tissues .

Given its significant role in carcinogenesis, FUBP1 is considered a potential therapeutic target for cancer treatment. Inhibitors that block the activation of pathways mediated by FUBP1, such as the TGF-β/Smad pathway, have shown promise in reducing cancer cell proliferation and invasion in preclinical studies .