Analytical Data
-
Gene name
DDX53
- Application
-
Alternative Names
Cancer-associated gene protein Cancer/testis antigen 26 Short name: CT26 DEAD box protein 53 DEAD box protein CAGE CAGE
-
Species
Human
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q86TM3
-
Expression Region
1-631aa
-
Molecular Weight
76.2 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
DDX53, a member of the DEAD-box protein family, plays a crucial role in various cellular processes, including RNA metabolism, ribosome biogenesis, and the regulation of gene expression. These proteins are characterized by the presence of a conserved helicase domain, which is essential for their ATP-dependent unwinding of RNA structures. Research indicates that DDX53 is involved in the regulation of stress responses and may influence the stability and translation of specific mRNAs. Given its potential role in cellular stress responses and its association with various diseases, including cancer, there is growing interest in characterizing DDX53 through recombinant protein studies. The production of DDX53 as a recombinant protein enables the exploration of its biochemical properties, interactions with RNA and other proteins, and its functional impact within the cell. Furthermore, understanding the precise mechanisms by which DDX53 operates could illuminate its potential as a therapeutic target. Investigating the structural and functional characteristics of DDX53 could provide insights into its role in disease etiology and offer new avenues for drug development. Thus, the research on DDX53 recombinant protein is essential for unveiling the biological significance of this helicase and its potential implications in health and disease.
