Analytical Data
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Gene name
GDA
- Application
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Alternative Names
CYPIN; Guanase; Guanine aminase; Guanine aminohydrolase; p51-nedasin
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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
Q9Y2T3
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Expression Region
Met1~Val454
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Molecular Weight
55kDa
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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
GDA, or guanine deaminase, is an enzyme that plays a crucial role in nucleotide metabolism by converting guanine into xanthine, which is then further processed into uric acid. The study of GDA and its recombinant forms has gained significant attention due to its potential applications in understanding various biological processes and developing therapeutic strategies for diseases related to purine metabolism, such as gout and certain types of cancer. Research on recombinant GDA protein focuses on its structural properties, enzymatic mechanisms, and interactions with other biomolecules. Utilizing techniques such as gene cloning, expression in host systems, and purification methods, scientists aim to produce GDA in sufficient quantities for detailed biochemical studies. Moreover, understanding the enzyme's kinetics and regulatory mechanisms can provide insights into how dysregulation of purine metabolism contributes to pathological conditions. Consequently, recombinant GDA research not only enhances our fundamental knowledge of metabolic pathways but also opens avenues for novel drug development, making it an important area of investigation in biotechnology and medical research.
