Analytical Data
-
Gene name
SRSF9
- Application
-
Alternative Names
SRSF9；SFRS9；SRP30C；Serine/arginine-rich splicing factor 9
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q13242
-
Expression Region
1-221aa
-
AA Sequence
MSGWADERGGEGDGRIYVGNLPTDVREKDLEDLFYKYGRIREIELKNRHGLVPFAFVRFEDPRDAEDAIYGRNGYDYGQCRLRVEFPRTYGGRGGWPRGGRNGPPTRRSDFRVLVSGLPPSGSWQDLKDHMREAGDVCYADVQKDGVGMVEYLRKEDMEYALRKLDDTKFRSHEGETSYIRVYPERSTSYGYSRSRSGSRGRDSPYQSRGSPHYFSPFRPY
-
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, which is crucial for the regulation of pre-mRNA splicing, a fundamental process in gene expression. Research on SRSF9 has gained prominence due to its involvement in various cellular processes, including alternative splicing, mRNA stability, and transport. Abnormal expression of SRSF9 has been linked to several diseases, including cancer, where it may contribute to the dysregulation of splicing patterns that ultimately affect cell proliferation and survival. Furthermore, studies have revealed that SRSF9 can interact with multiple RNA-binding proteins and other splicing factors, highlighting its role as a coordinator in the splicing machinery. Recent advancements in molecular biology techniques have enabled researchers to explore the structural and functional aspects of SRSF9, providing deeper insights into its role in the spliceosome and the regulation of gene expression. Understanding the mechanisms by which SRSF9 operates could potentially lead to novel therapeutic strategies aimed at correcting splicing anomalies in disorders associated with its dysregulation. Consequently, the recombinant expression of SRSF9 protein is pivotal for biochemical studies, enabling researchers to investigate its properties and interactions in vitro, thus advancing our comprehension of its biological significance.
