Recombinant Human WBP1 protein

WBP1 (WW Domain-Binding Protein 1), also known as PAWR or PRKCABP, is a multifunctional protein involved in diverse cellular processes, including apoptosis, transcriptional regulation, and protein-protein interactions. It was initially identified through its interaction with the WW domain of the Yes-associated protein (YAP), a key regulator of the Hippo signaling pathway. Structurally, WBP1 contains multiple functional domains, such as a proline-rich region, a WW domain-binding motif, and a C-terminal PDZ-binding domain, enabling it to act as an adaptor molecule in signaling networks. Its role in apoptosis is particularly notable, as it can promote cell death by interacting with proteins like PKC and Fas, while also modulating pathways like the PI3K/AKT and MAPK cascades.

Recombinant WBP1 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells*) to produce purified, biologically active forms for research. This allows precise study of its molecular interactions and mechanisms. Studies highlight WBP1's dual role in cancer, where it can act as a tumor suppressor by inducing apoptosis in certain contexts but may also exhibit oncogenic properties depending on cellular conditions. Dysregulation of WBP1 has been linked to cancers, neurodegenerative diseases, and immune disorders, making it a potential therapeutic target. Recombinant WBP1 is widely used in biochemical assays, structural studies, and drug discovery to explore its regulatory functions and develop targeted therapies. Its ability to influence critical pathways underscores its importance in both basic research and translational medicine.