Nucleophosmin (human, recombinant)

Nucleophosmin is a nucleolar phosphoprotein that is involved in diverse biological processes, including ribosome maturation, DNA repair, and mitotic spindle assembly. It is highly post-translationally modified and composed of an oligomerization domain, which contains two nuclear export signals, three acidic domains, an intrinsically disordered region, which contains two nuclear localization signals, and a C-terminal RNA-binding domain. Nucleophosmin is ubiquitously expressed and shuttles between the nucleolus and cytoplasm, however, alternative splicing of NPM1 produces a variant that lacks the RNA-binding domain and nucleolar localization signal and is instead localized throughout the nucleus. Nucleophosmin has histone- and protein chaperone activity and plays a role in ribosome assembly and export, centrosome duplication, cell cycle control, the stress response, and embryogenesis. Knockdown of NPM1 inhibits protein synthesis and the nuclear export of the 40S, 60S, and 80S ribosomal subunits in vitro and knockout of NPM1 is embryonic lethal in mice. Nucleophosmin fusion proteins have been found in patients with acute promyelocytic leukemia or non-Hodgkin's lymphoma.Synonyms: NPM, NPM1, Nucleolar Phosphoprotein B23, Nucleolar Protein NO38, Numatrin. Purity: >60% estimated by SDS-PAGE. Source: Recombinant human N-terminal His-tagged nucleophosmin expressed in E. coli. Amino Acids: 2-294 (full length). MW: 34.7 kDa. Formulation: (Request formulation change), 50 mM HEPES, pH 7.8, with 150 mM sodium chloride and 10% glycerol. Host: E. coli. UniProt Accession #: P06748.