Render Target: STATIC
Render Timestamp: 2024-11-20T11:33:38.522Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-05 20:50:25.173
Product last modified at: 2024-11-08T13:00:12.983Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

NPM1 (C Mutant Specific) Antibody #17944

Filter:
  • 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

    For optimal ChIP results, use 10 μL of antibody and 10 μg of chromatin (approximately 4 × 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Chromatin IP 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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