NPM1 (C Mutant Specific) Antibody #17944
- WB
- IP
- ChIP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 38 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Chromatin IP | 1:50 |
Storage
Protocol
Specificity / Sensitivity
NPM1 (C Mutant Specific) Antibody recognizes endogenous levels of total NPM1 C mutant protein. This antibody may also detect a band around 220 kDa that likely corresponds to pentameric NPM1 C mutant protein. This antibody does not cross-react with wild-type NPM1 protein.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the mutated carboxy terminus of human NPM1 C mutant protein. Antibodies are purified by peptide affinity chromatography.
Background
Nucleophosmin (NPM1; also known as NPM, B23, numatrin, or NO38) is an abundant phosphoprotein primarily found in nucleoli. It has been implicated in several distinct cellular functions, including assembly and transport of ribosomes, cytoplasmic/nuclear trafficking, regulation of DNA polymerase α activity, centrosome duplication, and molecular chaperoning activities (1,2). The NPM1 gene is also known for its fusion with the anaplastic lymphoma kinase (ALK) receptor tyrosine kinase. The NPM1 portion contributes to transformation by providing a dimerization domain, which results in activation of the fused kinase (3,4). NPM1 is also the most frequently mutated gene in acute myeloid leukemia (AML) and accounts for nearly 30% of all cases (5). These AML subtypes, classified as NPM1-mutated AML, are characterized by mutations in NPM1’s C-terminus that disrupt its nucleolar localization sequence and cause mislocalization from the nucleolus to the cytoplasm (6). This cytoplasmic form of NPM1, commonly referred to as NPM1c, is exclusive to myeloid malignancies and is not found in other forms of cancer (7). These mutations are always heterozygous, and NPM1c functions in a dominant negative fashion by dimerizing with wild-type NPM1 and recruiting it to the cytoplasm (6,8). Interestingly, NPM1 mutations alone are not sufficient to drive leukemogenesis, and further research is required to fully elucidate the impact of these mutations on disease progression (9).
- Okuda, M. et al. (2000) Cell 103, 127-40.
- Takemura, M. et al. (1999) J Biochem 125, 904-9.
- Morris, S.W. et al. (1994) Science 263, 1281-4.
- Bischof, D. et al. (1997) Mol Cell Biol 17, 2312-25.
- Falini, B. et al. (2005) N Engl J Med 352, 254-66.
- Falini, B. et al. (2006) Blood 107, 4514-23.
- Zarka, J. et al. (2020) Genes (Basel) 11, .
- den Besten, W. et al. (2005) Cell Cycle 4, 1593-8.
- Vassiliou, G.S. et al. (2011) Nat Genet 43, 470-5.
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