Recombinant Mouse Nucleophosmin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9987P

Recombinant Mouse Nucleophosmin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-9987P
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Product Overview

Host Species Mouse
Accession Q61937
Synonym B23 MGC104254 NO38 NPM NPM_HUMAN NPM1 Nucleolar phosphoprotein B23 Nucleolar protein NO38 Nucleophosmin Nucleophosmin (nucleolar phosphoprotein B23 numatrin) nucleophosmin nucleoplasmin family member 1 Nucleophosmin/nucleoplasmin family member 1 Numatrin OTTHUMP00000161024 OTTHUMP00000161025 OTTHUMP00000223397 OTTHUMP00000223398
Description Recombinant Mouse Nucleophosmin Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 49 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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.
Subcellular Location Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families Nucleoplasmin family
Database References
Tissue Specificity Expressed in B-cells that have been induced to switch to various Ig isotypes.

Gene Functions References

  1. In the current study, we demonstrate the existence of a negative feedback loop through which an increased B23 expression suppresses ERalpha. Because suppression of ERalpha expression is a late event during estrogen-dependent endometrial tumorigenesis, the inhibition of nucleophisminmay represent a strategy to promote ERalpha re-expression that ultimately restores tumor sensitivity to hormonal therapy PMID: 27527851
  2. molecular complementarity underlies the higher frequency and significantly worse prognosis associated with NPM1c/FLT3-internal tandem duplications vs NPM1/NRAS-G12D-mutant acute myeloid leukemia (AML) and functionally confirm the role of HOXA genes in NPM1c-driven AML. PMID: 28835438
  3. NPM1 knockdown decreased NF-kappaB-mediated transcription of selected target genes by decreasing the recruitment of NF-kappaB p65 to the gene promoters. PMID: 28003476
  4. study suggests that although neurons need NPM1 for survival, an increase in its expression beyond physiological levels and its translocation to the cytoplasm leads to death through abortive cell cycle induction. PMID: 27510036
  5. The levels of B23 expression are directly regulated by EGR1. PMID: 26577150
  6. IDH2 and NPM1 mutations synergize in the development and maintenance of acute myeloid leukemia stem-like cells. PMID: 25795706
  7. a function of NPM1 in the spatial organization of nucleolus-associated heterochromatin through DNA methyltransferase DNMT3A PMID: 25349213
  8. The data presented here support a novel role for NPM1 as a multilevel modulator of the base excision repair pathway. PMID: 24648491
  9. The mechanism of G-CSF's neuroprotection may be related in part to attenuating neuronal apoptosis by NPM1. PMID: 24829950
  10. In conclusion, we successfully established xenotransplantation model of human FLT3-ITD (mut) /NPM1 (-) CN-AML in NOD/SCID mice. PMID: 23771655
  11. This in vivo model of Flt3/ITD+/NPMc+ leukemia closely recapitulates human disease and will therefore serve as a tool for the investigation of the biology of this common disease entity PMID: 24184354
  12. HOPS acts as a functional bridge in the interaction between NPM and p19(Arf) PMID: 22890319
  13. NPM-Bax interaction enhances mitochondrial Bax accumulation, organelle injury, and cell death. PMID: 23459946
  14. These results suggest that the down-regulation of the identified nucleophosmin proteins in QRsP-11 cells compared to QR-32 cells is possibly related to tumor malignant progression. PMID: 23267140
  15. Overexpression of Npm1 in mice results in myeloproliferation and implies a perturbation in hematopoietic microenvironment. PMID: 23226219
  16. The B23 regulates neuronal survival by preventing SIAH1-GAPDH death signaling under stress-induced conditions in the brain. PMID: 23027902
  17. the aberrant feed-forward pathway that keeps eIF4E and C/EBPalphap30 elevated in NPM1(+/-) cells contributes to the MDS phenotype associated with NPM1 deficiency. PMID: 22851180
  18. level of Npm1 expression has a role in regulating hematopoietic stem cell numbers in the bone marrow. PMID: 21979879
  19. A dual function of NPM1 in M-CSF-differentiated macrophages. PMID: 21876121
  20. propose that although the t(2;5) simultaneously reduces NPM1 allelic dosage and creates the NPM-ALK fusion protein, the two events do not cooperate in the pathogenesis of anaplastic large cell lymphoma in our mouse model PMID: 21709672
  21. The Tpt1-Npm1 complex as a novel marker for highly proliferating cells, and offer further insight into the network that controls cellular fate. PMID: 20505363
  22. Data show that Oct4, Sox2 and Nanog individually form complexes with nucleophosmin (Npm1) to control embryonic stem (ES) cell fate determination. PMID: 21076177
  23. the Cdk2/Cdk4/NPM pathway is a major guardian of centrosome dysfunction and genomic integrity. PMID: 19933848
  24. involvement of NPM/B23 in the acute response of mammalian cells to environmental stress, such as UV rays PMID: 12374805
  25. Involvement of CDK2/cyclin E and nucleophosmin/B23 in centrosome duplication PMID: 12429912
  26. overexpression in fused forme with ALK induced different types of malignant lymphomas in IL-9 transgenic mice PMID: 12555065
  27. identifed a multifunctional protein, B23 that strongly cross-reacts with a phospho-MEK antibody in mitotic cells; findings suggest a phsophorylation site on B23 may have a role in the regulation of mitotic B23 PMID: 15358159
  28. NPM in the nucleolus, ARF utilizes an additional mechanism of tumor suppression, one that is readily antagonized by Mdm2 PMID: 15485902
  29. essential developmental role for Npm, and implication of its functional loss in tumorigenesis and myelodysplastic syndrome pathogenesis PMID: 16007073
  30. Based on the sequence, bioinformatics analysis on genomic structure of nucleophosmin and the transcription factor binding sites in the NPM 5' flanking region were performed. PMID: 16018192
  31. NPM/B23 localizes between the paired centrioles of unduplicated centrosomes; inhibition of Crm1 nuclear export receptor results in both accumulation of cyclin E at centrosomes and efficient dissociation of NPM/B23 from centrosomes. PMID: 16297385
  32. B23 is a downstream effector of polyamines via phosphorylation by the protein kinase CK2 PMID: 16342411
  33. NPM plays an important role in hematopoiesis via mechanisms involving modulation of HSC/progenitor cell cycle progression and stress response PMID: 16608843
  34. The suppression of the proteolytic degradation of nucleophosmin was associated with LPS-induced RAW 264.7 murine macrophage cell activation. PMID: 16609939
  35. knock-down of Npm1 expression by this siRNA system was not only highly efficient, but also tetracycline- dose- and induction time-dependent. PMID: 16870143
  36. knockdown of NPM blocked the increases in Arf(-/-) ribosome output and osteoclast activity, demonstrating that these gains require NPM. PMID: 18070929
  37. a molecular mechanism of B23 in the mitotic inhibition of GCN5-mediated histone acetylation and transactivation. PMID: 18165222
  38. Npm1 acts as a haploinsufficient tumor suppressor in the hematopoietic compartment PMID: 18212245
  39. NPMc(+) acute myeloid leukemia represents a primary event rather than a transformation stage of NPMc(-) acute myeloid leukemia PMID: 18367491
  40. NPM-regulated ribosome export is a fundamental process in cell growth PMID: 18809582
  41. The p53-independent tumor suppressive functions of p19(Arf) may be mediated by its ability to antagonize Senp3, thereby inducing cell cycle arrest by abnormally elevating the cellular levels of SUMOylated proteins. PMID: 18948745
  42. NPM may protect cells from apoptosis by reducing the mitochondrial level of p53 PMID: 19366707
  43. Inhibiting Crm1 in early metaphase causes the formation of excess acentriolar spindle poles containing NuMA and B23, but does not affect centrosome numbers. PMID: 19522705
  44. Data demonstrate that the reduction in NPM protein expression blocks cellular growth and proliferation, whereas phosphorylation of NPM-Thr198 is not essential for NPM's capacity to drive cell cycle progression and proliferation. PMID: 19561638
  45. Npm1 may act as an alarmin: implications for sepsis are reported. PMID: 19581374


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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