Nucleophosmin/Npm1 Protein, Human (193a.a, His)

The nucleophosmin/Npm1 protein plays critical roles in ribosome biogenesis, centrosome duplication, protein chaperones, histone assembly, and cell proliferation. Npm1 is a key player in the cellular orchestra that promotes ribosome nuclear export, associates with nucleolar ribonucleoprotein structures, and interacts with single-stranded nucleic acids. Nucleophosmin/Npm1 Protein, Human (193a.a, His) is the recombinant human-derived Nucleophosmin/Npm1 protein, expressed by E. coli , with N-His labeled tag. The total length of Nucleophosmin/Npm1 Protein, Human (193a.a, His) is 293 a.a., with molecular weight of ~34 kDa.

Nucleophosmin/Npm1 protein stands at the crossroads of diverse cellular processes, orchestrating pivotal roles in ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, and the intricate regulation of cell proliferation. This multifaceted protein emerges as a key player in the cellular orchestra, binding to ribosomes to facilitate their nuclear export, associating with nucleolar ribonucleoprotein structures, and interacting with single-stranded nucleic acids. Functioning as a chaperonin, Npm1 collaborates with core histones H3, H2B, and H4, and stimulates the endonuclease activity of APEX1 on double-stranded DNA while inhibiting its activity on single-stranded RNA. Beyond its involvement in nucleolar processes, Npm1 regulates centrosome and centriole duplication, counteracts apoptosis, and modulates the transcriptional activity of MYC target genes in conjunction with MYC. The intricate web of interactions involves partners such as NSUN2, SENP3, RPS10, NEK2, ROCK2, BRCA2, RPGR, CENPW, EIF2AK2/PKR, CEBPA, DDX31, NOP53, LRRC34, RRP1B, NPM3, ALKBH2, and TTF1, underscoring the complexity and versatility of Npm1 in cellular functions.

Human

E. coli

N-His

P06748 (E2-L294)

4869  [NCBI]

Approximately 34 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.