Analytical Data
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基因名
add
- Application
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别名
Adenosine aminohydrolase
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P22333
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表达区间
1-333aa
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分子量
52.4 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
