Analytical Data
-
Gene name
TRA2B
- Application
-
Alternative Names
SRFS10; Htra2-beta; TRA2-BETA; TRA2B; Splicing Factor,Arginine/Serine-Rich 10; Transformer-2 protein homolog B
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P62995
-
Expression Region
Ser64~Pro204
-
Molecular Weight
19kDa
-
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
TRA2B, or Transformer 2 Beta, is a member of the Ser/Arg-rich (SR) protein family, implicated in various aspects of RNA metabolism, including splicing, stability, and transport. Research on TRA2B has garnered attention due to its critical role in the regulation of alternative splicing, a process that significantly contributes to proteomic diversity in eukaryotic cells. Alterations in TRA2B expression or function have been linked to several diseases, including cancer, highlighting its potential as a therapeutic target. Additionally, TRA2B interacts with multiple RNA elements and other splicing factors, making it a crucial player in the splicing machinery. Understanding the structural and functional dynamics of TRA2B through recombinant protein studies can provide insights into its role in splicing regulation and its implications in disease mechanisms. This research is particularly relevant in the context of advancing molecular therapies and improving our understanding of the complexities of gene expression regulation.
