Analytical Data
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Gene name
DICER1
- Application
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Alternative Names
DICER1;DICER;HERNA;KIAA0928;Endoribonuclease Dicer
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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
Q9UPY3
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Expression Region
全长
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AA Sequence
full
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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
DICER1 is a crucial enzyme in the RNA interference pathway, responsible for processing precursor microRNAs (miRNAs) into functional molecules that regulate gene expression. Its role in the biogenesis of small RNAs is essential for cellular functions, development, and response to environmental stimuli. Mutations or dysregulation of DICER1 have been linked to various types of cancer and developmental disorders, making it a significant target for biomedical research. Recent studies have identified a range of DICER1-related pathologies, including pleuropulmonary blastoma, cystic nephroma, and other tumors, which are often associated with germline mutations in the DICER1 gene. Notably, these findings highlight the importance of understanding DICER1's structural and functional mechanisms to illuminate its role in tumorigenesis and development. The recombinant expression of DICER1 proteins allows for the in-depth study of its enzymatic activity and interactions with RNA substrates, providing insights into its regulatory functions in various biological contexts. Thus, research on DICER1 recombinant proteins not only enhances our understanding of its molecular functions but also holds potential for therapeutic interventions targeting DICER1-related diseases. Understanding the enzyme’s structural properties, substrate specificity, and interaction with cofactors can pave the way for innovative approaches in cancer treatment and gene therapy.











