Analytical Data
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Gene name
AGT
- Application
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Alternative Names
AGT；AGT1；SPAT；Alanine--glyoxylate aminotransferase
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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
P01019
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Expression Region
44-427aa
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AA Sequence
VIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNS
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Molecular Weight
57.9kDa
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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 AGT (Allyl Group Transfer) recombinant proteins has gained significant traction in the field of biotechnology and molecular biology due to their crucial role in various biochemical processes and applications. AGT proteins are known for their ability to catalyze specific reactions in living organisms, making them valuable tools for enzyme engineering, drug development, and metabolic pathway optimization. With the advent of genetic engineering techniques, researchers have successfully manipulated the genes encoding AGT proteins to produce recombinant versions, allowing for enhanced stability, activity, and specificity. These engineered proteins can be utilized in synthetic biology applications, such as the creation of biosensors, biocatalysts, and therapeutic agents. Furthermore, understanding the structural and functional dynamics of AGT recombinant proteins provides insights into enzyme mechanisms and interactions, paving the way for innovative solutions in environmental bioremediation, renewable energy production, and pharmaceutical synthesis. As such, ongoing research into AGT recombinant proteins is essential for advancing both fundamental scientific knowledge and practical applications that address real-world challenges.
