Anti-NUP98 antibody [2H10] - BSA and Azide free

Supplementary info

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

Activity summary

The NUP98 protein also known as nucleoporin 98 plays an important role in cellular mechanics. It forms a part of the nuclear pore complex important for regulating nucleocytoplasmic transport. With an approximate mass of 98 kDa NUP98 expresses mainly in the nucleus across various cell types. Alternative splicing of the NUP98 gene can lead to different isoforms. In some research contexts NUP98 is also referred to by related terms such as NUP96. Its expression appears widespread in many tissues replacing or complementing other nucleoporins.

Biological function summary

The NUP98 protein contributes to nuclear-cytoplasmic transport processes as part of the nuclear pore complex. In association with other nucleoporins NUP98 acts in cargo transport between the nucleus and cytoplasm facilitating the movement of RNA and proteins. It also participates in the assembly and disassembly cycles of the nuclear pore complex (NPC). Known interactions include those with components like the 13C2 complex and other mRNA export factors. NUP98's function impacts NPC architecture and its transport efficiency.

Pathways

NUP98 has essential roles beyond mechanical transport. It integrates into the mRNA export pathway collaborating with proteins like CRM1 (exportin-1) to regulate mRNA export. Additionally it plays a role in gene expression regulation by binding to gene promoters involving pathways linked to protein synthesis and cell cycle regulation. Connections with histone modifications suggest its involvement in chromatin remodeling linking it further to the regulation of gene expression pathways.

Associated diseases and disorders

NUP98 associations are significant. It is implicated in certain hematological malignancies like acute myeloid leukemia (AML) where it forms fusion proteins with partners such as HOXA9 and NSD1. Genetic rearrangements involving NUP98 contribute to oncogenesis altering normal cell function. Other conditions including dysregulation in autoimmune diseases suggest potential links to aberrant signaling pathways. Understanding these disease links involves studying interactions with proteins like MLL another significant player in leukemia pathogenesis.