epitope mapping within an internal region of NPM3 of human origin
recommended for detection of NPM3 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
NPM3 Background Information Nucleoplasmin (NP) and nucleophosmin (also called B23) are nuclear chaperones that mediate the assembly of ribosomes. Their activities are mediated through the binding of basic proteins via their acidic domains. Nucleophosmin is more abundant in tumor cells than in normal resting cells. Specifically, stimulation of the growth of normal cells is accompanied by an increase in nucleophosmin protein level. The structure of the N-terminal domain of nucleoplasmin (NP-core) is an eight-stranded ∫ barrel that fits within a stable pentamer. Both NP and NP-core are competent to assemble large complexes that contain the four core histones. Nucleoplasmin 3 (NPM3) shares many physical characteristics with the nucleo-phosmin/nucleoplasmin family, including an acidic domain, multiple potential phosphorylation sites and a putative nuclear localization signal. NPM3 protein is an abundant and widely expressed protein with primarily nuclear localization. The NPM3 gene maps to human chromosome 10q24.31.
