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NPM1 Antibody
Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB |
|---|---|
| Primary Accession | P06748 |
| Reactivity | Human, Mouse |
| Host | Mouse |
| Clonality | Monoclonal |
| Calculated MW | H=33 KDa |
| Isotype | IgG1 |
| Antigen Source | Human |
| Gene ID | 4869 |
|---|---|
| Antigen Region | 1-274 aa |
| Other Names | NPM1;NPM; Nucleophosmin; Nucleophosmin; Nucleolar phosphoprotein B23; Nucleophosmin; Nucleolar protein NO38; Nucleophosmin; Numatrin |
| Dilution | WB~~1:1000 IHC-P~~1:25 |
| Target/Specificity | Purified His-tagged NPM1 protein was used to produced this monoclonal antibody. |
| Format | Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | NPM1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | NPM1 |
|---|---|
| Synonyms | NPM |
| Function | Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). |
| Cellular Location | Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Can shuttle between cytoplasm and nucleus. Co- localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis |
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Background
Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication.
References
Swaminathan V., et al. Mol. Cell. Biol. 25:7534-7545(2005).
Tago K., et al. Proc. Natl. Acad. Sci. U.S.A. 102:7689-7694(2005).
Bolli N., et al. Lancet Oncol. 7:350-352(2006).
Lu L., et al. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
Kalnine N., et al. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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