Analytical Data
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Gene name
NOL5A
- Application
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Alternative Names
Nucleolar protein 56. Nucleolar protein 5A
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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
O00567
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Expression Region
1-174 aa
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AA Sequence
MKEAMVQAEEAAAEITRKLEKQEKKRLKKEKKRLAALALASSENSSSTPEECEEMSEKPKKKKKQKPQEVPQENGMEDPSISFSKPKKKKSFSKEELMSSDLEETAGSTSIPKRKKSTPKEETVNDPEEAGHRSGSKKKRKFSKEEPVSSGPEEAVGKSSSKKKKKFHKASQED
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Molecular Weight
45.9 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
NOL5A, a member of the nucleolar family of RNA-binding proteins, has garnered significant interest in recent years due to its potential roles in cell proliferation, differentiation, and stress response. This protein is primarily located in the nucleolus, where it is involved in ribosome biogenesis and pre-rRNA processing. Dysregulation of NOL5A has been associated with various cancers, making it a candidate for further study in oncological research. Its ability to interact with multiple RNA molecules suggests it may play a crucial role in post-transcriptional regulation and cellular homeostasis. Recent advancements in protein expression and purification techniques have facilitated the development of recombinant NOL5A for functional assays and structural studies, providing insights into its mechanisms of action. Understanding the structural and functional properties of NOL5A could unveil novel therapeutic targets and strategies for cancer treatment. This research not only aims to elucidate the biological significance of NOL5A but also explores its potential as a biomarker for disease progression or response to therapy, emphasizing its relevance in contemporary biomedical research.
