Analytical Data
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Gene name
NOP58
- Application
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Alternative Names
Nucleolar protein 5
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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
1-529aa
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Molecular Weight
75.6 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
Related Products
Protein Description
NOP58 is a pivotal nucleolar protein that plays a crucial role in ribosome biogenesis and the regulation of cellular processes. It is a component of the small nucleolar ribonucleoprotein (snoRNP) complexes, which are essential for the modification and processing of pre-rRNA. Recent studies have highlighted the significance of NOP58 in various cellular functions, including transcription regulation, RNA processing, and cell proliferation. Aberrant expression of NOP58 has been linked to several cancers and other diseases, making it a potential biomarker and therapeutic target. Researchers are increasingly interested in understanding the molecular mechanisms underlying NOP58's functions, particularly its interactions with other proteins and RNAs within the nucleolus. The development of recombinant NOP58 proteins has facilitated advanced studies, allowing for the exploration of its structural properties and functional assays. By employing techniques such as X-ray crystallography and NMR spectroscopy, scientists aim to elucidate the protein's three-dimensional structure and its dynamics in physiological and pathological conditions. Insights gained from these research endeavors could enhance our understanding of nucleolar biology and lay the groundwork for novel therapeutic strategies targeting NOP58-related pathways in diseases.
