Analytical Data
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Gene name
NONO
- Application
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Alternative Names
NONO；NRB54；Non-POU domain-containing octamer-binding Protein
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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
Q15233
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Expression Region
1-471aa
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AA Sequence
MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY
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Molecular Weight
67.2 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
The NONO protein, an essential component of the non-canonical RNA splicing machinery, plays a crucial role in various cellular processes including transcription regulation, DNA repair, and RNA metabolism. It is part of the Drosophila NONO/SMN protein family, characterized by RNA-binding motifs that enable interactions with various RNA species and other protein partners. Research into NONO has intensified due to its implications in neurodevelopmental disorders and certain cancers, where aberrations in its expression or function can lead to pathological conditions. Studies have shown that NONO is involved in the formation of ribonucleoprotein complexes and contributes to the regulation of gene expression at both transcriptional and post-transcriptional levels. Moreover, its interactions with other splicing factors suggest a significant role in alternative splicing processes, thereby influencing protein diversity. Investigating the structural dynamics and functional pathways of NONO can shed light on its mechanistic roles in cellular homeostasis and disease. Enhanced understanding of NONO’s role could also pave the way for novel therapeutic strategies targeting its dysfunction in specific disease contexts, emphasizing the importance of continued research in this area.
