Analytical Data
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Gene name
SRSF3
- Application
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Alternative Names
SRSF3；SFRS3；SRP20；；Serine/arginine-rich splicing factor 3
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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
P84103
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Expression Region
1-85aa
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AA Sequence
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAF VEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEK
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Molecular Weight
35 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
SRSF3, a member of the serine/arginine-rich (SR) splicing factor family, plays a significant role in pre-mRNA splicing and gene expression regulation. Research has shown that SRSF3 is crucial for various cellular processes, including cell proliferation, differentiation, and response to stress. Dysregulation of SRSF3 has been implicated in several diseases, particularly cancer, where it can influence alternative splicing events that contribute to tumorigenesis and metastasis. Studies have revealed that SRSF3 interacts with other splicing factors and regulatory proteins, highlighting its role in coordinating the splicing machinery in response to specific cellular signals. Moreover, the modulation of SRSF3 activity can affect the expression of key oncogenes and tumor suppressors, making it a potential target for therapeutic intervention. Investigating the molecular mechanisms underlying SRSF3 function and its impact on splicing regulation is essential for understanding its role in normal biology and disease, paving the way for developing new strategies in cancer treatment and other related disorders. As such, SRSF3 recombinant protein research is vital for elucidating its functional properties and potential as a biomarker or therapeutic target in oncology and other fields.
