Product: Nucleophosmin Mouse Monoclonal Antibody
Catalog: BF8032
Description: Mouse monoclonal antibody to Nucleophosmin
Application: WB IHC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 37kDa; 33kD(Calculated).
Uniprot: P06748

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Mouse
Application:
WB 1:500-1:3000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Monoclonal [AFfirm8032(AFP21825)]
Specificity:
Nucleophosmin Antibody detects endogenous levels of total Nucleophosmin.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

B23; MGC104254; NO38; NPM; NPM_HUMAN; NPM1; Nucleolar phosphoprotein B23; Nucleolar protein NO38; Nucleophosmin (nucleolar phosphoprotein B23 numatrin); Nucleophosmin; nucleophosmin nucleoplasmin family member 1; Nucleophosmin/nucleoplasmin family member 1; Numatrin; OTTHUMP00000161024; OTTHUMP00000161025; OTTHUMP00000223397; OTTHUMP00000223398;

Immunogens

Immunogen:

A synthesized peptide derived from human Nucleophosmin.

Uniprot:
Gene(ID):
Description:
NPM1 a nucleolar protein associated with nucleolar ribonucleoprotein structures and that binds single-stranded nucleic acids. Is a major component of template activating factor (TAF)-III. It plays a role in controlling centrosome duplication, and may function in the assembly and/or transport of the ribosome. Two alternatively spliced isoforms have been described.
Sequence:
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL

PTMs - P06748 As Substrate

Site PTM Type Enzyme
M1 Acetylation
S4 Phosphorylation P34947 (GRK5) , Q9NYY3 (PLK2) , P53350 (PLK1) , Q9H4B4 (PLK3)
S10 Phosphorylation
Y17 Phosphorylation
K24 Acetylation
K24 Ubiquitination
K27 Acetylation
K27 Sumoylation
K27 Ubiquitination
Y29 Phosphorylation
K32 Acetylation
K32 Sumoylation
K32 Ubiquitination
S43 Phosphorylation
R45 Methylation
S48 Phosphorylation
K54 Acetylation
K54 Sumoylation
K54 Ubiquitination
Y67 Phosphorylation
S70 Phosphorylation P24941 (CDK2) , P51955 (NEK2) , P06493 (CDK1)
K73 Sumoylation
K73 Ubiquitination
T75 Phosphorylation
T78 Phosphorylation
K80 Ubiquitination
S82 Phosphorylation
T86 Phosphorylation
S88 Phosphorylation P51955 (NEK2)
T95 Phosphorylation
R101 Methylation
S106 Phosphorylation
S112 Phosphorylation
S125 Phosphorylation O14965 (AURKA) , Q13535 (ATR)
S137 Phosphorylation
S139 Phosphorylation
K141 Acetylation
K141 Methylation
K141 Sumoylation
K141 Ubiquitination
S143 Phosphorylation
S149 Phosphorylation
K150 Acetylation
K150 Sumoylation
K150 Ubiquitination
K154 Acetylation
K155 Acetylation
K155 Ubiquitination
K157 Ubiquitination
K189 Ubiquitination
K193 Ubiquitination
S195 Phosphorylation
R197 Methylation
T199 Phosphorylation P41279 (MAP3K8) , Q00534 (CDK6) , P24941 (CDK2) , P06493 (CDK1) , P11802 (CDK4)
K202 Sumoylation
K202 Ubiquitination
K212 Acetylation
S214 Phosphorylation
K215 Acetylation
K215 Sumoylation
S217 Phosphorylation
S218 Phosphorylation
T219 Phosphorylation P06493 (CDK1)
S222 Phosphorylation
K223 Acetylation
K223 Sumoylation
K223 Ubiquitination
S227 Phosphorylation
K229 Acetylation
K229 Sumoylation
K229 Ubiquitination
K230 Acetylation
K230 Sumoylation
T234 Phosphorylation P24941 (CDK2) , P06493 (CDK1)
T237 Phosphorylation P06493 (CDK1)
K239 Sumoylation
K239 Ubiquitination
S242 Phosphorylation
S243 Phosphorylation
K248 Acetylation
K248 Methylation
K248 Sumoylation
K248 Ubiquitination
K250 Acetylation
K250 Sumoylation
K250 Ubiquitination
S254 Phosphorylation
K257 Acetylation
K257 Sumoylation
K257 Ubiquitination
S260 Phosphorylation
K263 Sumoylation
K263 Ubiquitination
K267 Acetylation
K267 Sumoylation
K267 Ubiquitination
K273 Acetylation
K273 Methylation
K273 Ubiquitination
T279 Phosphorylation
K292 Acetylation
K292 Sumoylation
S293 Phosphorylation

Research Backgrounds

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. In complex with MYC enhances the transcription of MYC target genes.

PTMs:

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.

ADP-ribosylated.

Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at Ser-4 by PLK1 takes place during mitosis. Phosphorylated by CDK2 at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-199, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-199 phosphorylated form has higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to viral reactivation by reducing viral LANA levels.

Sumoylated by ARF.

Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36.

Subcellular 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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Decamer formed by two pentameric rings associated in a head-to-head fashion (By similarity). Disulfide-linked dimers under certain conditions. 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). Interacts with DDX31; this interaction prevents interaction between NPM1 and HDM2. Interacts with MYC; competitive with NOP53. Interacts with NOP53; the interaction is direct and competitive with MYC. Interacts with LRRC34 (By similarity). Interacts with RRP1B. Interacts with NPM3.

(Microbial infection) Interacts with hepatitis delta virus S-HDAg.

(Microbial infection) Interacts with HTLV1 Rex protein (via N-terminal nuclear localization signal).

Family&Domains:

Belongs to the nucleoplasmin family.

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