Analytical Data
-
Gene name
DDX39A
- Application
-
Alternative Names
DDX39A；DDX39;ATP-dependent RNA helicase DDX39A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O00148
-
Expression Region
2-427aa
-
AA Sequence
AEQDVENDLLDYDEEEEPQAPQESTPAPPKKDIKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQIEPVNGQVTVLVMCHTRELAFQISKEYERFSKYMPSVKVSVFFGGLSIKKDEEVLKKNCPHVVVGTPGRILALVRNRSFSLKNVKHFVLDECDKMLEQLDMRRDVQEIFRLTPHEKQCMMFSATLSKDIRPVCRKFMQDPMEVFVDDETKLTLHGLQQYYVKLKDSEKNRKLFDLLDVLEFNQVIIFVKSVQRCMALAQLLVEQNFPAIAIHRGMAQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIVFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNVAELPEEIDISTYIEQSR
-
Molecular Weight
55.9 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
DDX39A, a member of the highly conserved DEAD-box RNA helicase family, plays a crucial role in various cellular processes, including RNA metabolism, splicing, and ribosome biogenesis. Research on DDX39A has garnered significant attention due to its involvement in essential mechanisms that regulate gene expression and RNA processing. Its ATP-dependent helicase activity allows the unwinding of RNA structures, facilitating the assembly of ribonucleoprotein complexes necessary for translation and other vital processes. Furthermore, aberrations in DDX39A expression have been associated with several diseases, including cancers, where it may contribute to tumorigenesis through altered RNA processing pathways. The production of DDX39A recombinant protein is crucial for advancing our understanding of its biochemical properties and functional mechanisms. By creating this protein, researchers aim to perform in-depth studies, including binding assays, enzymatic activity assessments, and structural analyses. Such investigations will provide insights into the specific roles of DDX39A in RNA-related processes and its potential as a therapeutic target in malignancies. As knowledge of DDX39A continues to evolve, understanding its functional dynamics through recombinant studies could pave the way for novel approaches in the treatment of diseases linked to RNA dysregulation.
