Analytical Data
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Gene name
SFRS9
- Application
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Alternative Names
Serine/arginine-rich splicing factor 9. Pre-mRNA-splicing factor SRp30C. Splicing factor. arginine/serine-rich 9
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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
Q13242
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Expression Region
1-221 aa
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AA Sequence
MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
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Molecular Weight
51.9 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
SFRS9, a member of the serine/arginine-rich splicing factor family, plays a crucial role in the regulation of pre-mRNA splicing and has been implicated in various biological processes, including cell proliferation, differentiation, and apoptosis. The study of SFRS9 has gained traction due to its association with several diseases, notably cancer, where its dysregulation can lead to aberrant splicing events that contribute to tumorigenesis and metastasis. Understanding the structural and functional characteristics of SFRS9 is essential for elucidating its mechanisms of action in splicing regulation and its potential roles as a therapeutic target. Recent advances in recombinant protein technology have facilitated the expression and purification of SFRS9, enabling researchers to investigate its interactions with RNA and other splicing factors. Through biophysical assays and functional studies, scientists aim to uncover the nuances of SFRS9's function in the spliceosome, providing insights that could lead to novel strategies for manipulating splicing in disease contexts. Furthermore, the exploration of SFRS9's regulatory pathways and post-translational modifications may reveal additional layers of complexity, offering opportunities for targeted interventions in splicing-related disorders. Overall, the research on SFRS9 offers significant promise for enhancing our understanding of gene expression regulation and developing innovative therapeutic approaches.
