Recombinant Human NUP35 protein

NUP35 (Nucleoporin 35), also known as NUP53. is a critical component of the nuclear pore complex (NPC), a large protein assembly embedded in the nuclear envelope that regulates nucleocytoplasmic transport. As a member of the scaffold nucleoporins, NUP35 plays a structural and functional role in maintaining NPC architecture and mediating selective molecular trafficking between the nucleus and cytoplasm. It belongs to the NUP93-205 subcomplex, which forms the NPC’s inner ring structure, contributing to pore stability and interaction with transport factors.

The recombinant NUP35 protein is engineered using biotechnological methods, typically expressed in bacterial or mammalian systems (e.g., E. coli or HEK293 cells) to ensure proper folding and post-translational modifications. This engineered protein retains key functional domains, including its conserved α-helical regions and nucleoporin-specific motifs, enabling in vitro studies on its interactions with other NPC components (e.g., NUP93. NUP205) or transport receptors like importins/exportins. Researchers utilize recombinant NUP35 to investigate NPC assembly, nuclear envelope organization, and its role in diseases. For instance, mutations in NUP35 have been linked to cardiovascular abnormalities and certain cancers, where disrupted nucleocytoplasmic transport contributes to pathological signaling. Additionally, studies explore its involvement in cell cycle regulation, viral infection mechanisms (as some pathogens hijack NPCs for replication), and potential therapeutic targeting. The availability of recombinant NUP35 facilitates structural analyses (e.g., cryo-EM) and high-throughput screening for drug candidates aiming to modulate NPC function in disease contexts.