Analytical Data
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Gene name
DNASEX
- Application
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Alternative Names
DNASE1L1; DNAS1L1; XIB; DNase-X; DNL1L; Deoxyribonuclease I-Like 1; Muscle-specific DNase I-like
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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
P49184
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Expression Region
Phe19~Ala302
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Molecular Weight
36kDa
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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
DNASEX, a recombinant protein derived from the DNase enzyme family, has attracted significant interest in biomedical research due to its role in enzymatic DNA fragmentation. Originally identified for its potential applications in molecular biology and clinical diagnostics, DNASEX is particularly notable for its ability to degrade extracellular DNA, which is often implicated in various pathological conditions, including autoimmune diseases and cancer. Researchers have been investigating the therapeutic implications of this protein, particularly in contexts where the removal of excess or damaged DNA could mitigate disease progression. Additionally, the recombinant nature of DNASEX allows for controlled production and modification, facilitating studies on its biochemical properties and enhancing its efficacy as a therapeutic agent. Understanding the structure-function relationship of DNASEX is crucial for its application in targeted therapies, providing insights into its potential use as a treatment for conditions characterized by impaired DNA clearance or excessive inflammation. Overall, the study of DNASEX holds promise not only for elucidating fundamental biological processes but also for developing innovative therapeutic strategies in medicine.
