Analytical Data
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Gene name
BAR/Phosphinothricin N-acetyltransferase
- Application
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Alternative Names
Phosphinothricin-resistance protein
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Species
Streptomyces hygroscopicus
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16426
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Expression Region
1-183aa
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Molecular Weight
22.6 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 BAR (Bialaphos Acetyltransferase) and Phosphinothricin N-acetyltransferase (PAT) recombinant proteins is of significant interest due to their vital role in conferring herbicide resistance in genetically modified plants. BAR, derived from the soil bacterium *Streptomyces hygroscopicus*, is capable of acetylating bialaphos, a naturally occurring herbicide, thereby allowing plants to survive in the presence of this toxic compound. PAT, on the other hand, is an important enzyme that inactivates phosphinothricin—a potent herbicide found in several agricultural applications. The ability to engineer crops with these recombinant proteins enhances agricultural productivity by providing robust weed control without damaging the crops themselves. As global agricultural practices face increasing pressure from herbicide-resistant weeds and the need for sustainable farming, the use of BAR and PAT provides an effective solution. The development and characterization of recombinant BAR and PAT proteins not only deepen our understanding of their enzymatic mechanisms but also facilitate the design of crops with improved productivity and resilience against herbicides. Moreover, the study of these proteins contributes to advancements in biotechnology, ensuring food security while minimizing environmental impacts. Research in this area continues to explore the optimization of these enzymes’ functions and their practical applications in various crop species, further shaping the future of herbicide-resistant agriculture.
