Anti-Nucleophosmin [NA24]
Invented by Dr Jacqueline Cordell at University of Oxford
Catalogue Number | 154830 |
Applications | N/A |
Antigen/Gene or Protein Targets | Nucleophosmin |
Synonyms | Nucleolar Phosphoprotein B23; Nucleolar Protein NO38; Numatrin; NPM; Nucleophosmin/Nucleoplasmin Family; Testicular Tissue Protein Li 128; B23 |
Reactivity | Human |
Relevance |
Recombinant antibody with use in understanding various nucleophosmin mutations and their associated diseases. Background and Research Application Nucleophosmin (NPM) also called B23, nutramin and NO38 is a ubiquitously expressed phosphoprotein involved in ribosome assembly/transport, cytoplasmic/nuclear trafficking, regulation of DNA polymerase alpha activity and centrosome duplication. It is also a crucial regulator of p53; it is involved in the acute response of mammalian cells to environmental stress, such as UV rays. NPM continuously shuttles between the nucleus and cytoplasm. NPM also localises between the paired centrioles of the centrosome and dissociates upon the phosphorylation of on Thr199 by CDK2/cyclin E prior to the initiation of centrosome duplication, an essential process for successful chromosome segregation during mitosis. The down-regulation of this protein results in the abnormal amplification of centrosomes which suggests that this protein may act as a suppressor of centrosome duplication. Aberrations involving nucleophasmin are found in multiple conditions, for instance in a form of non-Hodgkin lymphoma or acute promyelocytic leukaemia. This is a recombinant version of the anti NPM (NA24) monoclonal antibody. The epitope for this antibody lies within the N-terminal of NPM. It reacts with both WT-NPM and NPM-ALK, staining nuclei of neoplastic cells and providing diffuse cytoplasmic labelling. |
Host | Mouse |
Immunogen | Nucleophosmin recombinant protein |
Subclass | IgG1 |
Research Area | Epigenetics & Nuclear Signalling |
Immunogen UniProt ID | P06748 |
Notes |
Production Details Purified using multi-step affinity chromatography with protein A. Storage Conditions Store at -20 degrees frozen. Avoid repeated freeze/thaw cycles. Points of Interest NE24 antibody was used to perform immunohistochemical staining confirming that anaplastic large-cell lymphoma involves expression of mutated NPM-ALK fusion. Western Blot (WB) 1:100-1:500 Immunohistochemistry (Paraffin) (IHC (P)) 1:50-1:100 Flow Cytometry (FACS) 2 ug/test Concentration 1mg/ml as standard |
Cordell et al. 1999. Blood. 93(2):632-42. PMID: 9885226.
Detection of normal and chimeric nucleophosmin in human cells.
Finkbeiner et al. 2011. EMBO J. 30(6):1067-78. PMID: 21326211.
Gascoyne et al. 2016. Endocrinology. :en20161802. PMID: 28001444.
Gimenez et al. 2010. Proteomics. 10(15):2812-21. PMID: 20533335.
mTOR signaling regulates nucleolar targeting of the SUMO-specific isopeptidase SENP3.
Proteomic analysis of low- to high-grade astrocytomas reveals an alteration of the expression level of raf kinase inhibitor protein and nucleophosmin.
Raman et al. 2014. Mol Cell Biol. 34(24):4474-84. PMID: 25288641.
The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex.
Vitamin D Receptor Expression in Plasmablastic Lymphoma and Myeloma Cells Confers Susceptibility to Vitamin D.
Cordell et al. 1999. Blood. 93(2):632-42. PMID: 9885226.
Detection of normal and chimeric nucleophosmin in human cells.
Finkbeiner et al. 2011. EMBO J. 30(6):1067-78. PMID: 21326211.
Gascoyne et al. 2016. Endocrinology. :en20161802. PMID: 28001444.
Gimenez et al. 2010. Proteomics. 10(15):2812-21. PMID: 20533335.
mTOR signaling regulates nucleolar targeting of the SUMO-specific isopeptidase SENP3.
Proteomic analysis of low- to high-grade astrocytomas reveals an alteration of the expression level of raf kinase inhibitor protein and nucleophosmin.
Raman et al. 2014. Mol Cell Biol. 34(24):4474-84. PMID: 25288641.
The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex.
Vitamin D Receptor Expression in Plasmablastic Lymphoma and Myeloma Cells Confers Susceptibility to Vitamin D.