Analytical Data
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Gene name
NOP5
- Application
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Alternative Names
Nucleolar protein 58. Nucleolar protein 5
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y2X3
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Expression Region
1-529 aa
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AA Sequence
MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASAKLSELLPEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQTSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGVENRAKLEARLRTLEDRGIRKISGTGKALAKTEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEQVDKEDEITEKKAKKAKIKVKVEEEEEEKVAEEEETSVKKKKKRGKKKHIKEEPLSEEEPCTSTAIASPEKKKKKKKKRENED
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Molecular Weight
86 kDa
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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
NOP5, also known as NOP56, is a ribonucleoprotein that plays a crucial role in the biogenesis of ribosomal RNA and the assembly of ribosomes, essential processes for protein synthesis in all eukaryotic cells. Recent studies have highlighted its significance in various cellular functions, including cell proliferation, stress response, and the regulation of gene expression. Given its involvement in ribosome biogenesis, NOP5 is of particular interest in cancer research, as abnormalities in ribosomal components are often linked to tumorigenesis and cancer progression. Moreover, NOP5's interaction with other nucleolar proteins hints at its potential role in the coordination of cellular stress responses and ribosomal integrity. The reconstitution and characterization of NOP5 as a recombinant protein are essential for understanding its structural and functional properties. This research can pave the way for investigating NOP5's potential targets for therapeutic intervention, especially in cancer where its regulatory pathways may become altered. By studying NOP5 in a controlled laboratory setting, researchers aim to elucidate its mechanism of action, further delineate its role in ribosome assembly, and explore its implications in diseases associated with ribosomal dysfunction. Ultimately, this work contributes to the broader understanding of nucleolar function and its importance in cellular homeostasis and disease mechanisms.
