|ELISA (ELISA)||1-2 µg/mL|
|Immunocytochemistry (ICC)||2-10 µg/mL|
|Immunofluorescence (IF)||2-10 µg/mL|
|Immunohistochemistry (IHC)||Assay Dependent|
|Immunoprecipitation (IP)||10 µg|
|Western Blot (WB)||1-3 µg/mL|
|Immunohistochemistry (IHC)||See 3 publications below|
|Western Blot (WB)||See 32 publications below|
|Immunoprecipitation (IP)||See 3 publications below|
|Immunocytochemistry (ICC)||See 18 publications below|
|Miscellaneous PubMed (MISC)||See 23 publications below|
|Immunofluorescence (IF)||See 4 publications below|
|Tested Species reactivity||Human, Mouse, Rat|
|Published species reactivity||Virus , Non-human primate , Human , Mouse|
|Host / Isotype||Mouse / IgG1|
|Immunogen||NPM/B23 purified from rat hepatoma.|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
This antibody reacts with the C-terminus of Nucleophosmin (B23). Positive controls used: HeLa, K562, Jurkat, MCF-7, and HL60 cell lysates). In western blots the antibody recognizes a band at ~37 kDa.
Nucleophosmin (NPM) also called B23, nutramin, and NO38, is a ubiquitously expressed nucleolar phosphoprotein that accumulates in the nucleoplasm of cells. The putative function of NMP is ribosome assembly and transport. It is associated with pre-ribosomal particles and is localized in the granular region of the nucleolus. NPM is also involved in cytoplasmic/nuclear trafficking, regulation of DNA polymerase alpha activity, centrosome duplication, and regulation of p53. NPM continuously shuttles between the nucleus and cytoplasm. It has been shown to bind nucleic acid, prevent protein aggregation via its chaperon activities, protect enzymes during thermal denaturation, and facilitate renaturation of chemically denatured proteins. In its cellular structure role, there is evidence suggesting NPM is associated with the centrosome. It is the substrate of CDK2/cyclin E during duplication of centrosomes (cellular division). Due to the NPM gene interaction with several tumor-associated chromosome translocations, NPM is thought to be a portion of several fusion proteins: NPM-ALK, NPM-RAR, and NPM-MLF1. While it is not thought to be part of the transforming potential of these fusion proteins, it is believed to act as the interface for oligomerization and oncogenic conversion of these tumor-promoting fusion proteins. NMP has been found to be abundant in tumor-growing cells as compared to normal resting cells. In addition, NPM has also been found to shift from the nucleoli to the nucleoplasm when cells are exposed to certain anticancer drugs. Studies indicate applications of NPM to include: cellular nucleolar marker and determination of anticancer drug-effects, apoptosis, and detection of drug-resistant cells by NPM-translocation assay.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: NPM; NPM1; Nucleolar phosphoprotein B23; nucleolar protein B23.1; Nucleolar protein NO38; Nucleophosmin; nucleophosmin (nucleolar phosphoprotein B23, numatrin); nucleophosmin 1; nucleophosmin/nucleoplasmin family, member 1; Numatrin; testicular tissue protein Li 128
Gene Aliases: B23; B23NP; NO38; NPM; NPM1
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