Analytical Data
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Gene name
AADAT
- Application
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Alternative Names
AADAT；KAT2；KYAT2；Kynurenine/alpha-aminoadipate 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
Q8N5Z0
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Expression Region
30-425aa
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AA Sequence
PKSMISLAGGLPNPNMFPFKTAVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQLIKESL
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Molecular Weight
60.2 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
AADAT (Aminoadipate aminotransferase) is a pivotal enzyme involved in the lysine degradation pathway, which plays a crucial role in amino acid metabolism. Recent research has highlighted the significance of AADAT in various physiological processes, including neurotransmitter synthesis and cellular signaling. Its dysfunction has been linked to neurological disorders and metabolic dysregulation, prompting scientists to investigate its structural and functional characteristics. The study of AADAT's recombinant protein is crucial for understanding its enzymatic mechanisms and interactions at a molecular level. By producing AADAT in a recombinant system, researchers aim to obtain sufficient quantities of the enzyme for detailed kinetic analyses and structural studies. This could ultimately lead to insights into its role in health and disease, with potential applications in developing therapeutic strategies targeting related metabolic disorders. Moreover, elucidating the three-dimensional structure of AADAT through methods like X-ray crystallography would provide valuable information about its active site and substrate specificity, thus contributing to the bioengineering of enzymes with tailored functions for industrial applications. Overall, the research into AADAT recombination protein aligns with the broader goal of understanding complex metabolic pathways and their implications in human health.
