Analytical Data
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Gene name
add
- Application
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Alternative Names
Adenosine aminohydrolase
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Species
Escherichia coli
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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
P22333
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Expression Region
1-333aa
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Molecular Weight
52.4 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
Related Products
Protein Description
The study of ADD (Ataxia-telangiectasia mutated, DSB repair protein) recombinant proteins has garnered significant attention due to its crucial role in DNA damage response and repair mechanisms. ADD plays an essential part in maintaining genomic stability by facilitating the repair of double-strand breaks (DSBs) in DNA, which can occur due to various factors such as ionizing radiation, chemical agents, and normal cellular processes. Deficiencies or mutations in ADD are linked to severe genetic disorders, including ataxia-telangiectasia, characterized by neurodegeneration, immunodeficiency, and increased cancer risk. Researchers are increasingly focused on engineering recombinant ADD proteins to understand their structural and functional properties, optimize their activity in DNA repair pathways, and assess their potential therapeutic applications. The ability to produce these proteins in a controlled environment allows for detailed studies of their interactions with other cellular components involved in DSB repair. Furthermore, the exploration of ADD as a target for drug development offers promising avenues for cancer therapy, particularly in stratified medicine where specific mutations in the DNA repair machinery can inform treatment strategies. The ongoing research aims not only to unravel the complexities of ADD function but also to leverage its mechanisms for innovative therapeutic interventions, thereby addressing the challenges posed by genomic instability and its associated disorders.
