Analytical Data
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Gene name
DDP1
- Application
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Alternative Names
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase Short name: Ap6A hydrolase Diadenosine and diphosphoinositol polyphosphate phosphohydrolase 1 Diadenosine hexaphosphate hydrolase (AMP-forming)
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Species
Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99321
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Expression Region
2-188aa
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Molecular Weight
37.4 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
DDP1 (Dipeptidyl Peptidase 1) is an important serine protease that plays a crucial role in various biological processes, including immune response, cellular signaling, and tissue remodeling. It is primarily expressed in immune cells and has been implicated in the activation of pro-proteins and the modulation of inflammation. The study of DDP1 recombinant proteins has gained significant attention due to its potential therapeutic applications, such as in the treatment of autoimmune diseases and cancer. Recombinant technology allows for the production of DDP1 proteins in controlled environments, facilitating detailed studies of their structure-function relationships and biochemical properties. Researchers are focusing on elucidating the enzymatic mechanisms of DDP1, exploring its substrate specificity, and understanding its regulation within the immune system. Advances in molecular biology techniques, including CRISPR and protein engineering, are further enhancing our ability to manipulate and study this enzyme. Consequently, DDP1 has become a target for drug discovery, with efforts aimed at designing specific inhibitors to modulate its activity for therapeutic benefits. Understanding the biological significance and therapeutic potential of DDP1 recombinant proteins is essential for developing novel strategies to combat various diseases, thereby positioning DDP1 as a promising candidate for future biomedical research.
