Analytical Data
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Gene name
DNase I
- Application
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Alternative Names
DNaseI; DNL1; DRNI; DNase-I; Dornase alfa
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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
P24855
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Expression Region
Gly19~Ala259
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Molecular Weight
28kDa
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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
Recombinant DNase I is an important protein widely studied for its role in molecular biology and biotechnology applications. This enzyme, derived from the pancreas of bovine and other sources, specializes in degrading DNA, thereby playing a crucial role in various physiological processes, including apoptosis and immune response. Research into recombinant DNase I has gained prominence due to its therapeutic potential, particularly in the treatment of genetic disorders and inflammatory diseases, where excessive DNA can trigger detrimental immune responses. Advances in genetic engineering technologies have enabled the production of recombinant DNase I with enhanced specificity and efficiency. Furthermore, its applications extend beyond therapy; for instance, it is used in clearing DNA from protein samples, improving the accuracy of assays, and in the development of DNA-based vaccines. Understanding the structural and functional characteristics of recombinant DNase I aids in optimizing its production, enhancing its stability, and expanding its utility in research and clinical settings. Overall, the study of recombinant DNase I not only exemplifies the intersection of basic research and applied science but also underscores its significance in the advancement of therapeutic strategies and biotechnological innovations.
