Analytical Data
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Gene name
SNUPN
- Application
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Alternative Names
SNUPN;RNUT1;SPN1;Snurportin-1
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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
O95149
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Expression Region
1-360aa
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AA Sequence
MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS TPKLKGSSHS PDHPGCLMEN
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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
SNUPN (suppressor of nuclear receptor activity) is a crucial protein involved in various cellular processes, including gene expression regulation and cellular signaling. Its key functions center around influencing the activity of nuclear receptors, which play essential roles in mediating responses to hormones and other signaling molecules. The study of SNUPN has gained attention due to its potential implications in various diseases, including cancer, where dysregulation of nuclear receptor activity can lead to uncontrolled cell proliferation and survival. Given its multifunctional role, researchers have focused on understanding the molecular mechanisms underlying SNUPN interactions and function. The reconstitution of SNUPN as a recombinant protein provides a valuable tool for studying its structure-function relationships and interactions with other biomolecules. This enables scientists to conduct in-depth analyses of its role in nuclear receptor signaling pathways, as well as its involvement in cellular stress responses and other physiological processes. Exploring SNUPN through recombinant techniques not only enhances our comprehension of its biological functions but also contributes to identifying potential therapeutic targets for diseases associated with nuclear receptor dysregulation. Furthermore, manipulating SNUPN's activity may offer innovative strategies to restore normal cellular functions in pathological conditions, thus underscoring the importance of SNUPN in biomedical research.
