Nucleophosmin (NPM1), also known as nucleolar phosphoprotein B23, nucleolar protein NO38, or numatrin, is a multifunctional protein that plays a crucial role in various cellular processes. It is predominantly located in the nucleolus but can shuttle between the nucleus and the cytoplasm. Nucleophosmin is involved in ribosome biogenesis, centrosome duplication, and the regulation of the ARF-p53 tumor suppressor pathway.
Nucleophosmin is a highly conserved protein with multiple domains that facilitate its diverse functions. It contains an N-terminal oligomerization domain, a central acidic region, and a C-terminal nucleic acid-binding domain. These domains enable nucleophosmin to interact with various proteins and nucleic acids, contributing to its role in ribosome assembly and stress responses.
Nucleophosmin is frequently overexpressed in various cancers, including acute myeloid leukemia (AML), where it is often mutated. The NPM1 mutation leads to the aberrant cytoplasmic localization of the protein, which disrupts its normal functions and contributes to leukemogenesis. As a result, nucleophosmin has become a significant biomarker and therapeutic target in cancer research.
The mouse anti-human nucleophosmin antibody is a monoclonal antibody specifically designed to detect human nucleophosmin. Monoclonal antibodies are produced by identical immune cells that are clones of a unique parent cell, ensuring high specificity and consistency in targeting the antigen. This antibody is widely used in various applications, including immunocytochemistry (ICC), flow cytometry (Flow Cyt), and western blotting (WB).