Analytical Data
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Gene name
DCP1A
- Application
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Alternative Names
Smad4-interacting transcriptional co-activator Transcription factor SMIF
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NPI6
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Expression Region
1-582aa
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Molecular Weight
67.3 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
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Protein Description
DCP1A, or Decapping Enzyme 1A, is a crucial protein involved in the regulation of mRNA metabolism and degradation. It plays a significant role in the decapping process, which is essential for the subsequent hydrolysis of mRNA by exonucleases. Understanding DCP1A is particularly important given its implications in various cellular processes, including gene expression regulation, RNA turnover, and the response to stress conditions. Dysregulation of decapping enzymes like DCP1A has been implicated in numerous diseases, including cancer and neurodegenerative disorders, highlighting the necessity for in-depth studies on its structure and function. Recent advancements in biophysical and structural biology techniques have facilitated the detailed characterization of DCP1A, unveiling its interaction with other components of the mRNA decay machinery. This research is paving the way for potential therapeutic interventions targeting DCP1A, aiming to modulate its activity and restore normal cellular functions. Furthermore, insights gained from studying DCP1A can contribute to the broader understanding of RNA metabolism and its critical roles in health and disease.
