Analytical Data
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Gene name
Nucleophosmin/Npm1
- Application
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Alternative Names
B23; NPM; Nucleolar Phosphoprotein B23; Numatrin; Nucleophosmin/Nucleoplasmin Family,Member 1; Nucleolar protein NO38
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q61937
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Expression Region
Gly20~Lys154
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Molecular Weight
18kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Nucleophosmin (NPM1) is a highly conserved nucleolar phosphoprotein that plays a crucial role in various cellular processes, including ribosome biogenesis, cell proliferation, and stress responses. It is primarily localized in the nucleolus and shuttles between the nucleus and cytoplasm, highlighting its importance in nucleocytoplasmic transport. Mutations in the NPM1 gene, especially in the context of acute myeloid leukemia (AML), have been extensively studied due to their impact on oncogenesis and disease progression. The most common mutation, NPM1c, results in a protein that lacks its C-terminal domain, leading to aberrant localization and loss of its regulatory functions. Research on recombinant NPM1 protein has gained momentum as it provides valuable insights into the structural and functional aspects of the protein, offering potential therapeutic targets for AML. Studies utilizing recombinant NPM1 facilitate the understanding of its interactions with other cellular proteins and its role in the assembly of ribonucleoprotein complexes. Moreover, given that NPM1 is involved in various cellular pathways such as cell cycle regulation and apoptosis, recombinant protein studies offer a platform for exploring its involvement in cancer biology and the development of novel cancer treatments. Understanding NPM1’s precise biological functions and its contribution to disease mechanisms through recombinant model systems is essential for advancing targeted therapies in NPM1-mutated malignancies.
