Analytical Data
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Gene name
SRSF1
- Application
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Alternative Names
ASF; SF2; SFRS1; Splicing Factor 2; Splicing Factor,Arginine/Serine-Rich 1; Alternate Splicing Factor; Alternative Splicing Factor; pre-mRNA-splicing factor SF2, P33 subunit
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q07955
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Expression Region
Cys16~Arg224
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Molecular Weight
27kDa
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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, or Serine/Arginine-Rich Splicing Factor 1, is a crucial member of the serine/arginine-rich protein family, playing a vital role in pre-mRNA splicing and gene regulation. Research highlights that SRSF1 influences alternative splicing events, thereby impacting diverse processes such as cell proliferation, differentiation, and apoptosis. Elevated levels of SRSF1 have been linked to several types of cancers, including breast cancer and leukemia, underscoring its potential as a biomarker and therapeutic target. Furthermore, SRSF1 interacts with various splicing factors and RNA-binding proteins, contributing to a complex regulatory network that fine-tunes gene expression. Its role in splicing regulation extends to the modulation of cancer-related isoforms, making it a critical focus of investigation in understanding tumorigenesis. Recent studies utilizing recombinant SRSF1 proteins have facilitated the exploration of its function and interactions at the molecular level, paving the way for innovative strategies in cancer treatment and personalized medicine. The ongoing research seeks to elucidate the precise mechanisms by which SRSF1 exerts its effects on splicing and gene expression, emphasizing its significance in both basic biology and clinical applications.
