Analytical Data
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Gene name
DCP2
- Application
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Alternative Names
DCP2；NUDT20；m7GpppN-mRNA hydrolase
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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
Q8IU60
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Expression Region
1-385aa
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AA Sequence
METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFY MQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTY GAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETG FDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWF SIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSD NGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKP YNNHSEMSDLLKGKKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAE GQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL
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Molecular Weight
68 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
DCP2 (Decapping Protein 2) is a crucial enzyme involved in mRNA decay, playing a significant role in post-transcriptional regulation of gene expression. It catalyzes the removal of the protective 7-methylguanylate cap structure from the mRNA, marking it for degradation. The regulation of mRNA stability and degradation by DCP2 is essential for various cellular processes, including development, differentiation, and response to environmental changes. Dysregulation of DCP2 has been implicated in various diseases, including cancer, neurodegenerative disorders, and viral infections, highlighting its potential as a therapeutic target. Research into the structure, function, and regulatory mechanisms of DCP2 is critical for understanding its role in cellular physiology and pathology. Recent advances in recombinant protein expression techniques have facilitated the production of DCP2 at scale, allowing for detailed biochemical and structural studies. These studies aim to elucidate the molecular mechanisms through which DCP2 interacts with other proteins, RNA substrates, and cofactors, thus providing insights into the intricate pathways of mRNA metabolism. Understanding DCP2's functions and regulations could lead to innovative approaches in treating diseases linked to mRNA dysregulation.
