Analytical Data
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Gene name
DDX19A
- Application
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Alternative Names
DDX19A；DDX19L；ATP-dependent RNA helicase DDX19A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NUU7
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Expression Region
1-478aa
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AA Sequence
MATDSWALAVDEQEAAVKSMTNLQIKEEKVKADTNGIIKTSTTAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPMMLAEPPQNLIAQSQSGTGKTAAFVLAMLSRVEPSDRYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
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Molecular Weight
70.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
DDX19A, a member of the DExD/H-box RNA helicase family, plays a crucial role in various cellular processes, including RNA metabolism, splicing, and the regulation of gene expression. As an ATP-dependent helicase, it unwinds RNA structures and is instrumental in processing pre-mRNA and facilitating ribosome assembly. Recent studies have highlighted its involvement in the cellular stress response and its potential links to several diseases, including cancer and viral infections. The functional characterization of DDX19A is essential for understanding its mechanisms in RNA biology and its implications in pathophysiology. Given its pivotal role, recombinant DDX19A protein has become a focus of research, aimed at elucidating its structural properties and interactions with RNA and other cellular partners. Investigating this protein can provide insights into its enzymatic activity and potential as a therapeutic target. Additionally, assessing the effects of mutations or dysregulation of DDX19A could further reveal its contributions to disease mechanisms. Overall, research on DDX19A recombinant protein is crucial for advancing our understanding of RNA helicases and developing new strategies for disease intervention.
