Analytical Data
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Gene name
SRSF2
- Application
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Alternative Names
SRSF2；SFRS2；Serine/arginine-rich splicing factor 2
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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
Q01130
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Expression Region
1-221aa
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AA Sequence
MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS
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Molecular Weight
25.4 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
Related Products
Protein Description
SRSF2 (Serine/Arginine Rich Splicing Factor 2) is a member of the serine/arginine-rich (SR) protein family, which plays a critical role in pre-mRNA splicing and regulation of gene expression. This protein is essential for the splicing process, where introns are removed from precursor mRNA, resulting in the formation of mature mRNA that can be translated into proteins. Mutations in the SRSF2 gene have been linked to various hematological malignancies, particularly myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML), highlighting its importance in cancer biology. Recent studies have indicated that SRSF2 mutations can lead to aberrant splicing of key oncogenes and tumor suppressors, thereby contributing to tumorigenesis. Understanding the functional implications of SRSF2 and its role in splicing regulation may provide insights into potential therapeutic targets for treating cancers associated with its mutations. Moreover, research into SRSF2's interactions with other splicing factors and its recruitment to spliceosomes is crucial for elucidating the complex mechanisms underlying mRNA processing. The development of recombinant SRSF2 proteins for biochemical assays and structural studies can further advance our understanding of its splice regulatory functions and inform the design of targeted therapies in the context of SRSF2-driven malignancies.
