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NPM1 Antibody

Purified Mouse Monoclonal Antibody (Mab)

     
  • 1 - NPM1 Antibody AP53282
    Western blot detection of NPM1 in Hela,Jurkat and 3T3 cell lysates using NPM1 mouse mAb (1:1000 diluted).Predicted band size:33KDa.Observed band size:38KDa.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB
Primary Accession P06748
Reactivity Human, Mouse
Host Mouse
Clonality Monoclonal
Isotype IgG1
Calculated MW 38 KDa
Additional Information
Gene ID 4869
Other Names B23;MGC104254;NMP1;NO38;NPM 1;NPM;NPM_HUMAN;NPM1;Nucleolar Phosphoprotein B23;Nucleolar protein NO38;Nucleophosmin (nucleolar phosphoprotein B23 numatrin);Nucleophosmin; Nucleophosmin/B23.2;Nucleophosmin/nucleoplasmin family member 1;Nucleoplasmin Family Member 1;Numatrin;OTTHUMP00000161024;OTTHUMP00000161025;OTTHUMP00000223397; OTTHUMP00000223398;TRK fused gene.
Dilution WB~~1:1000
Format Purified mouse monoclonal in buffer containing 0.1M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.02% sodium azide, 50%,glycerol
Storage Store at -20 °C.Stable for 12 months from date of receipt
Protein Information
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.
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
Research Areas

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. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation.

REFERENCES

Chan W.-Y.,et al.Biochemistry 28:1033-1039(1989).
Li X.,et al.Biochem. Biophys. Res. Commun. 163:72-78(1989).
Zhang X.T.,et al.Biochem. Biophys. Res. Commun. 164:176-184(1989).
Chan P.-K.,et al.Nucleic Acids Res. 25:1225-1232(1997).
Okuwaki M.,et al.Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.

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