Recombinant Human PURB protein

**Background of PURB Recombinant Protein**

PURB (Purine-rich element-binding protein B) is a member of the PUR protein family, which includes transcription and translation regulators involved in diverse cellular processes. This family, characterized by conserved purine-rich binding domains, plays roles in DNA replication, RNA metabolism, and chromatin remodeling. PURB specifically interacts with single-stranded purine-rich DNA/RNA motifs, modulating gene expression and genomic stability. It is implicated in cell cycle regulation, differentiation, and stress responses, with emerging links to cancer, neurodegenerative diseases, and developmental disorders.

Recombinant PURB protein is engineered using expression systems (e.g., *E. coli* or mammalian cells*) to produce purified, functional protein for *in vitro* studies. Its recombinant form retains DNA/RNA-binding activity, enabling researchers to dissect molecular mechanisms, such as how PURB regulates target genes or interacts with partners like PURA (Purα) or nucleic acids. Tags (e.g., His-, GST-) are often added to facilitate purification and detection.

Studies utilizing recombinant PURB have advanced understanding of its role in transcriptional repression, mRNA localization, and chromatin organization. For example, PURB is shown to suppress oncogene transcription in cancer models and influence neuronal RNA transport in neurodegenerative contexts. Its dysregulation is associated with pathologies like glioblastoma and Alzheimer’s disease, highlighting its therapeutic potential.

As a research tool, recombinant PURB supports assays such as electrophoretic mobility shift assays (EMSAs), co-immunoprecipitation, and cell-based functional studies. Its availability accelerates exploration of PURB's biological significance and its interplay with cellular pathways, offering insights into disease mechanisms and targeted interventions.