Analytical Data
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Gene name
NPM2
- Application
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Alternative Names
NPM2;Nucleoplasmin-2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q86SE8
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Expression Region
1-214aa
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AA Sequence
MNLSSASSTE EKAVTTVLWG CELSQERRTW TFRPQLEGKQ SCRLLLHTIC LGEKAKEEMH RVEILPPANQ EDKKMQPVTI ASLQASVLPM VSMVGVQLSP PVTFQLRAGS GPVFLSGQER YEASDLTWEE EEEEEGEEEE EEEEDDEDED ADISLEEQSP VKQVKRLVPQ KQASVAKKKK LEKEEEEIRA SVRDKSPVKK AKATARAKKP GFKK
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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
Related Products
Protein Description
NPM2 (Nucleophosmin 2) is a nucleolar protein that plays a crucial role in various cellular processes, including ribosome biogenesis, cell proliferation, and stress response. Recent studies have highlighted its importance in developmental biology and its potential involvement in various diseases, particularly cancer. The ability of NPM2 to bind RNA and other proteins suggests that it may function as a critical regulator of gene expression and RNA metabolism. Research into the recombinant production of NPM2 proteins has gained traction due to the need for understanding its molecular mechanisms and interactions in vivo. Producing NPM2 in a recombinant form allows researchers to investigate its structure, function, and interaction with other cellular components in a controlled environment. Moreover, studying the biochemical properties of NPM2, such as its post-translational modifications and binding affinities, can reveal insights into its role in tumorigenesis and cellular stress responses. As a result, developing reliable methods for the purification and characterization of NPM2 provides valuable tools for exploring its biological functions and potential therapeutic implications. This growing body of research underscores the significance of NPM2 not only in fundamental biology but also in the development of innovative strategies aimed at targeting this protein in disease contexts.
