Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- HRP Rabbit monoclonal [EP1857Y] to Nucleophosmin (phospho T199)
- Suitable for: Dot blot, WB
- Reacts with: Human
- Conjugation: HRP
Product nameHRP Anti-Nucleophosmin (phospho T199) antibody [EP1857Y]
See all Nucleophosmin primary antibodies
DescriptionHRP Rabbit monoclonal [EP1857Y] to Nucleophosmin (phospho T199)
Tested applicationsSuitable for: Dot blot, WBmore details
Species reactivityReacts with: Human
Synthetic peptide within Human Nucleophosmin (phospho T199). The exact sequence is proprietary.
- WB: HEK-293 treated with Calyculin A.
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In preparation for this, we have started to update the applications & species that this product is Abpromise guaranteed for.
We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
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Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle. Store In the Dark.
Storage bufferpH: 7.40
Preservative: 0.1% 10% Proclin 300 Solution
Constituents: PBS, 30% Glycerol, 1% BSA
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab202879 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/50000. Detects a band of approximately 33 kDa (predicted molecular weight: 33 kDa).|
FunctionInvolved 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).
Involvement in diseaseA chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated.
A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA.
A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1.
Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.
Sequence similaritiesBelongs to the nucleoplasmin family.
modificationsAcetylated at C-terminal lysine residues, thereby increasing affinity to histones.
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.
Cellular localizationNucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. 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.
- Information by UniProt
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All lanes : HRP Anti-Nucleophosmin (phospho T199) antibody [EP1857Y] (ab202879) at 1/50000 dilution
Lane 1 : Untreated HEK-293 (Human epithelial cell line from embryonic kidney) whole cell lysates
Lane 2 : HEK-293 (Human epithelial cell line from embryonic kidney) treated with 0.1 µM Calyculin A for 60 minutes whole cell lysates
Lane 3 : HEK-293 (Human epithelial cell line from embryonic kidney) treated with 0.1 µM Calyculin A for 60 minutes whole cell lysates. Then the membrane was incubated with Alkaline phosphatase.
Lysates/proteins at 15 µg per lane.
Predicted band size: 33 kDa
Additional bands at: 38 kDa. We are unsure as to the identity of these extra bands.
Exposure time: 1 second
Blocking buffer: 5% NFDM/TBST
Diluting buffer: 5% NFDM/TBST
ab202879 binding Nucleophosmin (phospho T199) in Dot blot at a dilution of 1/1000.
Lane 1: Nucleophosmin phospho T199 peptide
Lane 2: Nucleophosmin non-phospho peptide
Exposure time: 10 seconds
Diluting buffer: 5%NFDM/TBST
Blocking buffer: 5%NFDM/TBST
ab202879 has not yet been referenced specifically in any publications.