Analytical Data
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Gene name
nahG
- Application
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Alternative Names
nahG；Salicylate hydroxylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23262
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Expression Region
2-434aa
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AA Sequence
KNNKLGLRIGIVGGGISGVALALELCRYSHIQVQLFEAAPAFGEVGAGVSFGPNAVRAIVGLGLGEAYLQVADRTSEPWEDVWFEWRRGSDASYLGATIAPGVGQSSVHRADFIDALVTHLPEGIAQFGKRATQVEQQGGEVQVLFTDGTEYRCDLLIGADGIKSALRSHVLEGQGLAPQVPRFSGTCAYRGMVDSLHLREAYRAHGIDEHLVDVPQMYLGLDGHILTFPVRNGGIINVVAFISDRSEPKPTWPADAPWVREASQREMLDAFAGWGDAARALLECIPAPTLWALHDLAELPGYVHGRVVLIGDAAHAMLPHQGAGAGQGLEDAYFLARLLGDTQADAGNLAELLEAYDDLRRPRACRVQQTSWETGELYELRDPVVGANEQLLGENLATRFDWLWNHDLDTDLAEARARLGWEHGGGGALRQG
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Molecular Weight
54.3 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
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.
