Analytical Data
-
Gene name
SRSF9
- Application
-
Alternative Names
Pre-mRNA-splicing factor SRp30CSplicing factor, arginine/serine-rich 9
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q13242
-
Expression Region
1-221aa
-
Molecular Weight
52.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SRSF9 (Serine/Arginine-Rich Splicing Factor 9) is a member of the SR protein family that plays a crucial role in mRNA splicing, regulation, and various aspects of gene expression. Research on SRSF9 has gained significance due to its involvement in alternative splicing, which is a key mechanism that expands the proteomic diversity of genes. Dysregulation of splicing factors like SRSF9 has been implicated in several diseases, including cancer, where aberrant splicing patterns can promote tumorigenesis and metastasis. Studies have shown that SRSF9 interacts with pre-mRNA, influencing the selection of splice sites, and thus impacting the production of protein isoforms. This makes SRSF9 a potential target for therapeutic interventions aimed at correcting splicing defects. Recent advancements in the understanding of the structural and functional aspects of SRSF9, including its phosphorylation and interactions with other splicing factors, could provide insights into its regulatory mechanisms. Additionally, the development of recombinant SRSF9 proteins allows for detailed studies of its splicing activity and interactions, facilitating the exploration of its role in both normal cellular processes and disease states. Understanding SRSF9's functions and regulatory pathways could contribute to identifying new biomarkers for diseases and developing novel treatments that target splicing mechanisms.
