Analytical Data
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Gene name
Adenosine Deaminase/ADA
- Application
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Alternative Names
Adenosine Aminohydrolase
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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 95% as determined by SDS-PAGE.
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Uniprot
P00813
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Expression Region
Lys11~Val280
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Molecular Weight
33kDa
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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
Adenosine deaminase (ADA) is an essential enzyme that catalyzes the irreversible deamination of adenosine to inosine, playing a critical role in purine metabolism and regulating extracellular adenosine levels, which are vital for various physiological processes. Deficiencies in ADA can lead to severe immune deficiencies, as observed in ADA-SCID (severe combined immunodeficiency), underscoring its importance in maintaining immune system function. Research on recombinant ADA protein has gained momentum in recent years, particularly due to its potential therapeutic applications in treating ADA deficiency and other related disorders. The use of recombinant DNA technology allows for the production of large quantities of functional ADA, facilitating the investigation of its biochemical properties and therapeutic effects. Advances in protein engineering have also enabled the development of modified versions of ADA with enhanced stability and activity, further expanding its potential use in clinical settings. Furthermore, the exploration of ADA as a target for immunomodulation in cancer therapy has opened new avenues for research, positioning recombinant ADA not only as a critical enzyme in metabolic regulation but also as a promising candidate in the fields of gene therapy and oncology.
