Analytical Data
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Gene name
SNFT
- Application
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Alternative Names
Basic leucine zipper transcriptional factor ATF-like 3. B-ATF-3. 21 kDa small nuclear factor isolated from T-cells. Jun dimerization protein p21SNFT
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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
Q9NR55
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Expression Region
1-127 aa
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AA Sequence
MSQGLPAAGSVLQRSVAAPGNQPQPQPQQQSPEDDDRKVRRREKNRVAAQRSRKKQTQKADKLHEEYESLEQENTMLRREIGKLTEELKHLTEALKEHEKMCPLLLCPMNFVPVPPRPDPVAGCLPR
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Molecular Weight
40.9 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
SNFT (small nuclear F-tract) is a type of small noncoding RNA that has recently gained attention in research for its potential implications in gene expression regulation and cellular metabolism. This protein plays a crucial role in the splicing process of pre-mRNA, which is an essential step in gene expression. Dysfunction or aberrations in SNFT protein levels have been linked to various diseases, including certain cancers and neurodegenerative disorders. Researchers are investigating the structural properties and functional roles of SNFT to better understand its involvement in these pathological conditions. The study of SNFT reconstituted proteins aims to elucidate the mechanisms by which they interact with other cellular components and regulate splicing. This research is pivotal for developing targeted therapeutic strategies that could potentially correct or mitigate the effects of gene expression dysregulation. Furthermore, understanding the dynamics of SNFT could contribute to the broader field of RNA biology, offering insights into how noncoding RNAs influence gene regulatory networks. Overall, the exploration of SNFT and its reconstitution holds promise for advancing our knowledge in molecular biology and therapeutic applications.
