Analytical Data
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基因名
D62T,T68A
- Application
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种属
Human immunodeficiency virus 1
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9DKF2
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表达区间
1-107aa(D62T,T68A)
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分子量
18.0 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 recombinant proteins D62T and T68A is rooted in the exploration of protein engineering and its applications in biotechnology and medicine. These specific mutations, derived from a particular protein of interest, have been hypothesized to impact the protein's stability, function, and interactions. D62T, a substitution of aspartic acid with threonine at position 62, is expected to enhance certain biochemical properties, while T68A, involving an alanine replacement at position 68, may affect its structural conformation and activity. Understanding these mutations is crucial, as they can provide insights into the underlying mechanisms of protein function and facilitate the development of novel enzymes or therapeutics. By utilizing techniques such as site-directed mutagenesis and expression in suitable host systems, researchers can analyze the effects of these modifications on enzyme kinetics, thermal stability, and substrate specificity. The potential applications range from industrial processes, such as biocatalysis, to therapeutic developments, where engineered proteins could offer improved efficacy and reduced side effects. Overall, the investigation of D62T and T68A serves not only to advance fundamental knowledge in protein science but also to harness the power of recombinant technology for practical solutions in various fields.
