Anti-Nucleoporin p62/NUP62 antibody [2A]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Nucleoporin p62 also known as NUP62 plays a significant role in transporting molecules across the nuclear envelope. This protein is a part of the nuclear pore complex which acts as a gateway for nucleocytoplasmic exchange. NUP62 has a molecular weight of approximately 62 kDa. It is expressed in the cell nucleus particularly at the nuclear envelope where it helps in the regulation of macromolecular traffic between the nucleus and cytoplasm.

Biological function summary

NUP62 is essential for maintaining the normal function of the nuclear pore complex. It forms a soluble subcomplex with other nucleoporins facilitating nuclear pore assembly. This protein contributes to the dynamic nature of the nuclear porins ensuring efficient and selective transport. NUP62 also interacts directly with nucleic acids and other transport receptors allowing for the precise regulation of nuclear-cytoplasmic exchange processes.

Pathways

NUP62 takes part in critical transport pathways such as the karyopherin-mediated import and export processes. It collaborates with importin-beta a transport receptor that binds to nuclear localization signals on cargo proteins. Through these pathways NUP62 ensures that essential proteins and RNAs are correctly swapped between the nucleus and the rest of the cell playing an important role in cellular homeostasis and gene expression regulation.

Associated diseases and disorders

Defects in NUP62 have been linked to conditions like neurodegenerative diseases and certain cancers. Anomalies in its function can disrupt normal cellular communication and lead to pathological states. NUP62 interacts with proteins implicated in these conditions such as amyloid precursor protein in Alzheimer's disease indicating its importance in neuronal function. In cancer altered expression of NUP62 can contribute to the dysregulation of gene expression which is a hallmark of tumorigenesis.