Analytical Data
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Gene name
SRSF1
- 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
SRSF1, a member of the serine/arginine-rich splicing factor family, plays a crucial role in pre-mRNA splicing and gene regulation. It is known for its involvement in alternative splicing, a process that enables cells to produce multiple protein isoforms from a single gene, thus contributing significantly to protein diversity and functional complexity. Dysregulation of SRSF1 has been implicated in various diseases, including cancer, where it promotes tumorigenesis by altering splicing patterns of oncogenes and tumor suppressor genes. Research into SRSF1 recombinant proteins has gained momentum as scientists aim to elucidate its specific functions and interactions at the molecular level. By producing SRSF1 in a recombinant form, researchers can accurately study its role in splicing mechanisms, identify its binding partners, and explore its potential as a therapeutic target. The production of SRSF1 recombinant protein enables the use of biochemical assays, structural studies, and high-throughput screening of small molecules, which could help in developing novel strategies to modulate its activity in pathological conditions. Understanding the dynamics of SRSF1 through recombinant studies holds the promise of advancing our knowledge of gene regulation and splicing mechanisms, unlocking new avenues for therapeutic interventions in diseases linked to splicing abnormalities.
