Analytical Data
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Gene name
SFRS10
- Application
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Alternative Names
arginine/serine-rich 10; Arginine/serine-rich splicing factor 10; hTRA2-beta; SFRS10; Splicing factor; Splicing factor arginine/serine rich 10; SRFS10; TRA-2 beta; TRA2-beta; Tra2b; TRA2B_HUMAN; TRAN2B; Transformer 2 beta homolog; Transformer-2 protein homolog B; Transformer-2 protein homolog beta; Transformer-2-beta
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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
P62995
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Expression Region
111-201 aa
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AA Sequence
RANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHT
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Molecular Weight
26.5 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
SFRS10, also known as splicing factor, arginine/serine-rich 10, is a protein that plays a crucial role in the regulation of pre-mRNA splicing and alternative splicing processes, essential for the production of diverse protein isoforms in eukaryotic cells. Its significance has been underscored in various biological contexts, including development, cell differentiation, and the cellular response to stress. Dysregulation of SFRS10 has been associated with several diseases, particularly cancer, where aberrant splicing patterns contribute to tumorigenesis and metastasis. Recent studies have focused on elucidating the molecular mechanisms through which SFRS10 interacts with spliceosomal components and other regulatory proteins, highlighting its involvement in the splicing machinery. Additionally, SFRS10's role in modulating the expression of various genes involved in critical pathways suggests it may serve as a potential therapeutic target or biomarker for certain malignancies. Researchers are now investigating the structural features and post-translational modifications of SFRS10 that influence its function, aiming to provide insights into how these mechanisms may be exploited for therapeutic interventions. The exploration of SFRS10 and its implications in splicing regulation thus presents a promising avenue for understanding fundamental cellular processes and advancing cancer treatment strategies.
