Analytical Data
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基因名
nahG
- Application
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别名
nahG；Salicylate hydroxylase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P23262
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表达区间
2-434aa
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氨基酸序列
KNNKLGLRIGIVGGGISGVALALELCRYSHIQVQLFEAAPAFGEVGAGVSFGPNAVRAIVGLGLGEAYLQVADRTSEPWEDVWFEWRRGSDASYLGATIAPGVGQSSVHRADFIDALVTHLPEGIAQFGKRATQVEQQGGEVQVLFTDGTEYRCDLLIGADGIKSALRSHVLEGQGLAPQVPRFSGTCAYRGMVDSLHLREAYRAHGIDEHLVDVPQMYLGLDGHILTFPVRNGGIINVVAFISDRSEPKPTWPADAPWVREASQREMLDAFAGWGDAARALLECIPAPTLWALHDLAELPGYVHGRVVLIGDAAHAMLPHQGAGAGQGLEDAYFLARLLGDTQADAGNLAELLEAYDDLRRPRACRVQQTSWETGELYELRDPVVGANEQLLGENLATRFDWLWNHDLDTDLAEARARLGWEHGGGGALRQG
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分子量
54.3 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
Nicotiana tabacum adenine glycosylase (nahG) is an important enzyme that facilitates the degradation of the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D) and other related compounds, making it a subject of significant interest in bioremediation studies. NahG has been widely studied due to its ability to confer resistance to certain harmful environmental pollutants, and researchers are exploring its potential applications in agricultural biotechnology and environmental management. Genetic engineering techniques have enabled the production of recombinant nahG proteins, which can be more efficiently produced and characterized compared to their native counterparts. These recombinant proteins can be utilized to enhance the detoxification processes in contaminated soils, thereby improving the ecological health of agricultural lands. Additionally, investigating the structure-function relationship of nahG aids in deciphering its catalytic mechanism and enhances the design of more effective biocatalysts. Recent advancements in molecular biology and protein engineering have further propelled research into optimizing nahG for various applications, including its integration into genetically modified crops that exhibit enhanced detoxification capabilities. Overall, the research on nahG recombinant proteins is pivotal for developing sustainable agricultural practices and mitigating pesticide pollution, contributing to a cleaner environment and promoting agricultural productivity.
