MP20001 Nucleophosmin Primary Antibody MP20001 [M7H10B9]
![MP20001 Nucleophosmin Primary Antibody MP20001 [M7H10B9]](https://mxbioscience.com/media/catalog/product/cache/1/image/9df78eab33525d08d6e5fb8d27136e95/p/0/p06748-npm1-structure.png)
![MP20001 Nucleophosmin Primary Antibody MP20001 [M7H10B9]](https://mxbioscience.com/media/catalog/product/cache/1/image/9df78eab33525d08d6e5fb8d27136e95/p/0/p06748-npm1-subcell.png)
Details
Application
| Application | FCM, WB, IHC, ELISA, ICC |
|---|---|
| ELISA | 1/10000 |
| ICC (Immunocytochemistry) | 1/100- 1/500 |
| FCM (Flow Cytometry) | 1/200 - 1/400 |
| IHC | 1/200 - 1/400 |
| WB (Cell Lysate) | 1/200 - 1/1000 |
Target
| UniProtKB | P06748 |
|---|---|
| Protein | Nucleophosmin |
| Gene | NPM1 |
| Organism | Homo sapiens (Human) |
| 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). |
| Molecular function | activating transcription factor binding chromatin binding core promoter binding histone binding NF-kappaB binding protein heterodimerization activity protein homodimerization activity protein kinase binding protein kinase inhibitor activity protein N-terminus binding ribosomal large subunit binding ribosomal small subunit binding RNA binding rRNA binding Tat protein binding transcription coactivator activity transcription factor binding unfolded protein binding |
| Biological process | cell aging cellular response to UV cell volume homeostasis CENP-A containing nucleosome assembly centrosome cycle chromatin remodeling DNA repair intracellular protein transport negative regulation of apoptotic process negative regulation of cell population proliferation negative regulation of centrosome duplication negative regulation of mRNA splicing, via spliceosome negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB nucleocytoplasmic transport Source: UniProtKB nucleosome assembly Source: UniProtKB positive regulation of cell cycle G2/M phase transition Source: UniProtKB positive regulation of cell population proliferation Source: UniProtKB positive regulation of centrosome duplication Source: Ensembl positive regulation of NF-kappaB transcription factor activity Source: UniProtKB positive regulation of protein kinase activity Source: Ensembl positive regulation of protein localization to nucleolus Source: Ensembl positive regulation of protein ubiquitination Source: Ensembl positive regulation of transcription, DNA-templated Source: UniProtKB positive regulation of transcription by RNA polymerase II Source: CAFA positive regulation of translation Source: UniProtKB protein localization Source: UniProtKB protein stabilization Source: Ensembl regulation of cell growth Source: Ensembl regulation of centriole replication Source: UniProtKB regulation of centrosome duplication Source: GO_Central regulation of DNA damage response, signal transduction by p53 class mediator Source: Ensembl regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB regulation of endodeoxyribonuclease activity Source: UniProtKB regulation of endoribonuclease activity Source: UniProtKB regulation of mRNA stability involved in cellular response to UV Source: UniProtKB regulation of transcription by RNA polymerase II Source: Reactome ribosomal large subunit biogenesis Source: GO_Central ribosomal large subunit export from nucleus Source: GO_Central ribosomal small subunit biogenesis Source: GO_Central ribosomal small subunit export from nucleus Source: GO_Central ribosome assembly Source: UniProtKB rRNA export from nucleus Source: GO_Central signal transduction Source: UniProtKB viral process Source: UniProtKB-KW |
| Protein names | Recommended name:Nucleophosmin Short name: NPM Alternative name(s): Nucleolar phosphoprotein B23 Nucleolar protein NO38 Numatrin |
| Gene names | Name:NPM1 Synonyms:NPM |
| Subcellular location | Nucleus;nucleolus;nucleoplasm;Cytoskeleton;centrosom 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. |
| Interaction | Decamer formed by two pentameric rings associated in a head-to-head fashion (By similarity). Disulfide-linked dimers under certain conditions (PubMed:25818168). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3. Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts with isoform 1 of NEK2. Interacts with ROCK2 and BRCA2. Interacts with RPGR. Interacts with CENPW. Interacts with EIF2AK2/PKR. Interacts with CEBPA (isoform 4) (PubMed:20075868). Interacts with DDX31; this interaction prevents interaction between NPM1 and HDM2 (PubMed:23019224). Interacts with MYC; competitive with NOP53 (PubMed:25956029). Interacts with NOP53; the interaction is direct and competitive with MYC (PubMed:25956029). Interacts with LRRC34 (By similarity). Interacts with RRP1B (PubMed:19710015, PubMed:20926688). Interacts with NPM3 (PubMed:22362753). (Microbial infection) Interacts with hepatitis delta virus S-HDAg. (Microbial infection) Interacts with HTLV1 Rex protein (via N-terminal nuclear localization signal). |
Sequence
There are 3 isoforms produced by alternative splicing
Isoform-1 Sequence
| Length | 294 |
|---|---|
| Mass (Da) | 32,575 |
| Sequence |
10 20 30 40 50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK
160 170 180 190 200
VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP
210 220 230 240 250
AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK
260 270 280 290
MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL
|
Isoform-2 Sequence
| Length | 265 |
|---|---|
| Mass (Da) | 29,465 |
| Sequence |
10 20 30 40 50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK
160 170 180 190 200
VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKGQESFK
210 220 230 240 250
KQEKTPKTPK GPSSVEDIKA KMQASIEKGG SLPKVEAKFI NYVKNCFRMT
260
DQEAIQDLWQ WRKSL
|
Isoform-3 Sequence
| Length | 259 |
|---|---|
| Mass (Da) | 28,400 |
| Sequence |
10 20 30 40 50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK
160 170 180 190 200
VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP
210 220 230 240 250
AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK
MQASIEKAH
|
| conjugations | N/A |
|---|---|
| host | mouse |
| antibody | Mouse Monoclonal antibody |
| modifications | N/A |
| reactivity | human, mouse, rat |
| presentation | 0.01% Sodium azide |
| purification | Protein A purified |
| storage | [-20°C] |
| target | Nucleophosmin |
| format | Liquid |
| clonality | [M7H10B9] |
| application | FCM, WB, IHC, ELISA, ICC |