Analytical Data
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Gene name
OAT
- Application
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Alternative Names
OAT;Ornithine 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
P04181
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Expression Region
26-439aa
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AA Sequence
TSVAT KKTVQGPPTS DDIFEREYKY GAHNYHPLPV ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA LKSQVDKLTL TSRAFYNNVL GEYEEYITKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIQKYKAKI VFAAGNFWGR TLSAISSSTD PTSYDGFGPF MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV PDPGYLMGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD KLGIILRNEL MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI KEDELRESIE IINKTILSF
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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
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Protein Description
OAT (Ornithine Aminotransferase) is a pivotal enzyme in the urea cycle and amino acid metabolism, predominantly located in the mitochondria of liver and kidney cells. Dysregulation or deficiency of OAT can lead to metabolic disorders, particularly in the context of hyperornithinemia, which can have severe neurological implications. OAT has gained attention in biotechnology for its potential therapeutic applications, especially in metabolic diseases. The focus of recent research has been on the recombinant production of OAT, which allows for substantial quantities of the enzyme to be produced for further study and potential clinical use. Advances in molecular biology techniques, such as gene cloning and expression systems, have enabled scientists to produce functional OAT in various host systems, including bacteria, yeast, and mammalian cells. This recombinant OAT can be used for enzyme replacement therapy, and studies are ongoing to explore its efficacy in restoring normal metabolic function in affected individuals. Additionally, understanding the structure-function relationship of the OAT enzyme at a molecular level is crucial for developing effective therapeutic strategies and for designing inhibitors or modulators that could be beneficial in conditions associated with OAT deficiency. Through concerted research efforts, the characterization and application of recombinant OAT hold promise for innovative treatments for metabolic disorders and contribute to our understanding of amino acid metabolism.
