Analytical Data
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Gene name
SFRS3
- Application
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Alternative Names
Serine/arginine-rich splicing factor 3. Pre-mRNA-splicing factor SRP20. Splicing factor. arginine/serine-rich 3
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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
P84103
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Expression Region
1-164 aa
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AA Sequence
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRSPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK
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Molecular Weight
45.7 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
SFRS3 (serine/arginine-rich splicing factor 3) is a member of the serine/arginine-rich splicing factor family, which plays a crucial role in mRNA splicing, post-transcriptional regulation, and gene expression. The protein is involved in the processing of pre-mRNA, influencing alternative splicing events that ultimately determine the maturation and stability of mRNA transcripts. Dysregulation of SFRS3 has been implicated in various diseases, including cancer, where alterations in splicing patterns can contribute to tumorigenesis and the progression of malignancies. Recent studies have highlighted the significance of SFRS3 in specific cellular contexts, particularly in the regulation of splicing events related to oncogenes and tumor suppressor genes. Research into SFRS3 has also revealed its potential as a therapeutic target, as modulating its activity could restore normal splicing patterns and counteract the aberrant gene expression associated with diseases. Understanding the structural and functional aspects of SFRS3, including its interactions with other splicing factors and RNA substrates, is essential for elucidating its precise role in cellular processes and the molecular mechanisms underlying its involvement in various pathologies. Current studies are focused on characterizing SFRS3 through methods such as recombinant protein expression, functional assays, and interaction studies, aiming to provide insights into its role in splicing regulation and its potential as a biomarker or therapeutic target in oncology.
