NFYC Polyclonal Antibody

CCAAT binding factor NF-Y is a heteromeric transcription factor that specifically binds to CCAAT sequences in many eukaryotic genes. NF-Y is made up of three subunits, NF-YA, NF-YB, and NF-YC. All three components are required for DNA binding. Within each NF-Y subunit, the segment necessary for the formation of the NF-Y-DNA complex is conserved from yeast to human.

These conserved segments are homologous to the histone-fold motif of eukaryotic histones. The DNA-binding domains of the NF-YB and NF-YC subunits have been suggested to interact via a protein-protein histone-fold "handshake" motif in a manner analogous to histone proteins, H2B and H2A, respectively.


The protein encoded by this gene is a subunit of a trimeric complex, forming a highly conserved transcription factor that binds with high specificity to CCAAT motifs in the promoter regions of a variety of genes. This gene product, the C subunit, forms a tight dimer with the B subunit (NFYB), a prerequisite for the association of the A subunit (NFYA).

The resulting trimer binds DNA with high specificity and affinity. The B and C subunits each contain a histone-like motif. The observation of the histone nature of these subunits is supported by two types of evidence; protein sequence alignments and experiments with mutants. Additional regulation, initially supported by the EST database, can be represented by alternative splicing in this subunit.[7]

Two microRNAs; miR-30c and miR-30e are located within the introns of the nfyc gene. These microRNAs are actively transcribed in human insulin-producing beta cells in pancreatic islets which also show high expression of nfyc and CDH1 genes.

Expression of these intronic microRNAs is essential to maintain the differentiated phenotype of human islet beta cells. Inhibition of miR-30 family microRNAs induces epithelial-mesenchymal transition of human pancreatic islet cells