Analytical Data
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Gene name
gabT
- Application
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Alternative Names
gabT；GABAT；4-aminobutyrate aminotransferase. mitochondrial
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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
P63505
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Expression Region
1-449aa
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AA Sequence
MASLQQSRRLVTEIPGPASQALTHRRAAAVSSGVGVTLPVFVARAGGGIVEDVDGNRLIDLGSGIAVTTIGNSSPRVVDAVRTQVAEFTHTCFMVTPYEGYVAVAEQLNRITPGSGPKRSVLFNSGAEAVENAVKIARSYTGKPAVVAFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEIYRAPLSYPYRDGLLDKQLATNGELAAARAIGVIDKQVGANNLAALVIEPIQGEGGFIVPAEGFLPALLDWCRKNHVVFIADEVQTGFARTGAMFACEHEGPDGLEPDLICTAKGIADGLPLSAVTGRAEIMNAPHVGGLGGTFGGNPVACAAALATIATIESDGLIERARQIERLVTDRLTTLQAVDDRIGDVRGRGAMIAVELVKSGTTEPDAGLTERLATAAHAAGVIILTCGMFGNIIRLLPPLTIGDELLSEGLDIVCAILADL
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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
GabT is a key enzyme involved in the synthesis of the amino acid gamma-aminobutyric acid (GABA), which plays a critical role in neurotransmission and is significant in various physiological processes, including mood regulation and muscle relaxation. The recombinant production of GabT has garnered attention due to its potential applications in biotechnology and pharmaceuticals. Understanding the structure and function of GabT can lead to enhanced biosynthesis of GABA, offering pathways for the development of novel therapeutic agents for neurological disorders such as anxiety and depression. Moreover, advancements in molecular cloning and expression systems have enabled researchers to produce large quantities of recombinant GabT for biochemical studies and industrial applications. This research not only highlights the enzyme’s mechanisms but also explores its stability, substrate specificity, and catalytic efficiency, leading to improved strategies for GABA production. As the demand for GABA and its derivatives increases in the food and pharmaceutical industries, the study of GabT as a recombinant protein presents a promising avenue for innovation and development in bioprocessing techniques.
