Analytical Data
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Gene name
SRSF3
- Application
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Alternative Names
Pre-mRNA-splicing factor SRP20;Splicing factor, arginine/serine-rich 3
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Species
Human
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Source
E. coli
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Tag
N- His-GB1
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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
1-86aa
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Molecular Weight
17.9 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, also known as serine/arginine-rich splicing factor 3, is a member of the serine/arginine-rich (SR) protein family, which plays a crucial role in the regulation of pre-mRNA splicing, RNA processing, and gene expression. This protein is known for its unique ability to shuttle between the nucleus and cytoplasm, influencing various aspects of RNA metabolism. Research has shown that SRSF3 is involved not just in splicing but also in alternative splicing events that significantly impact cellular functions and contribute to disease states. Dysregulation of SRSF3 has been implicated in several cancers, where it may promote oncogenic signaling pathways by altering the splicing patterns of key genes involved in cell proliferation and survival. Moreover, SRSF3 interacts with numerous RNA-binding proteins and participates in the formation of ribonucleoprotein complexes, highlighting its importance in post-transcriptional regulation. Investigating the recombinant protein of SRSF3 can provide insights into its structure-function relationships and reveal potential therapeutic targets for manipulating splicing processes in disease contexts. Understanding SRSF3's role in RNA biology may pave the way for novel strategies in cancer treatment and highlight its potential as a biomarker for disease progression. Overall, the study of SRSF3 and its recombinant form is essential for unraveling the complexities of RNA regulation and its implications in health and disease.
