Neuropilin-1 consists of several distinct domains:
The extracellular domain of mouse Neuropilin-1 shares a high degree of similarity with its counterparts in other species, including humans, rats, horses, cows, and dogs . This conservation across species underscores the protein’s fundamental role in physiological processes.
Recombinant mouse Neuropilin-1 is typically produced in a mouse myeloma cell line (NS0) and includes a C-terminal 6-His tag for purification purposes . The recombinant protein is often used in research to study its interactions with various ligands, such as VEGF and SEMA3A, and to explore its role in different biological processes.
The recombinant form of Neuropilin-1 is available in a carrier-free formulation, which means it does not contain bovine serum albumin (BSA). This is particularly useful for applications where the presence of BSA could interfere with experimental results .
Neuropilin-1 is a subject of extensive research due to its involvement in critical biological processes. Studies have shown that inhibiting Neuropilin-1 can lead to improved tumor growth inhibition in vivo, highlighting its potential as a therapeutic target in cancer treatment . Researchers have developed monoclonal antibodies that specifically bind to different domains of Neuropilin-1, blocking its interactions with ligands like VEGF and SEMA3A .