Analytical Data
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Gene name
SFRS1
- Application
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Alternative Names
SRSF1;ASF;SF2;SF2P33;Serine/arginine-rich splicing factor 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
Q07955
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Expression Region
2-248aa
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AA Sequence
SGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT
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Molecular Weight
43.6kDa
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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
SFRS1, or Serine/Arginine-rich Splicing Factor 1, is a crucial protein that plays a significant role in the regulation of pre-mRNA splicing, a process essential for gene expression and cellular function. Aberrant splicing often results in various diseases, including cancers, making SFRS1 a focal point for research in molecular biology and therapeutic development. Its multifunctional nature allows it to interact with several proteins and RNA molecules, influencing not only splicing but also other cellular processes such as stress response and cell cycle regulation. Given its involvement in diverse biological pathways, SFRS1 has garnered attention for its potential as a biomarker for disease states and as a target for innovative treatments. Recent studies have highlighted its relevance in tumorigenesis, suggesting that modulating SFRS1 activity could provide new avenues for cancer therapy. As the understanding of its molecular mechanisms expands, the recombinant production of SFRS1 protein becomes imperative for studying its structure-function relationships and for developing SFRS1-targeted therapeutic strategies. Thus, research into SFRS1 and its recombinant protein forms is vital for elucidating its roles in health and disease, paving the way for novel interventions in splicing-related disorders.
