FUBP1 Human
Description
FUBP1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
The Far Upstream Element Binding Protein 1 (FUBP1), also known as FBP1, is a crucial single-stranded DNA-binding protein that plays a significant role in the regulation of gene expression, particularly the c-Myc oncogene. This protein is encoded by the FUBP1 gene and is involved in various cellular processes, including transcription, translation, and RNA stability.
FUBP1 is a 644-amino acid protein with three well-defined domains:
- N-terminal domain: This amphipathic helix domain is thought to repress the activity of the C-terminal domain.
- Central domain: This domain is responsible for DNA binding.
- C-terminal domain: This transactivation domain contains three tyrosine-rich motifs and is involved in the activation of transcription .
FUBP1 regulates the expression of the c-Myc gene by binding to the far upstream element (FUSE) located upstream of the c-Myc promoter. This binding occurs on the non-coding strand and is crucial for the regulation of c-Myc in undifferentiated cells . The c-Myc gene is a proto-oncogene that controls the expression of about 10% of cellular genes, including those essential for cell proliferation, differentiation, and apoptosis .
In addition to its role in transcription, FUBP1 also acts as an RNA-binding protein. It regulates the translation or stability of several mRNA species, including those of GAP43, p27Kip, and nucleophosmin . FUBP1’s RNA-binding activity is also implicated in the replication of viral RNA from Hepatitis C and Enterovirus 71 .
Aberrant expression of FUBP1 has been found in various malignant tissues, indicating its role in carcinogenesis. Mutations in the FUBP1 gene or alternative splicing of its repressor FIR have been associated with multiple cancers . FUBP1 is also important for the development of certain organs, such as the lung and neural system .
