Analytical Data
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Gene name
BAAT
- Application
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Alternative Names
FLJ20300; BAAT; BAAT_HUMAN; BACAT; BAT; Bile acid CoA: amino acid N-acyltransferase (glycine N-choloyltransferase)
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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
Q14032
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Expression Region
1-418aa
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AA Sequence
MIQLTATPVS ALVDEPVHIR ATGLIPFQMV SFQASLEDEN GDMFYSQAHY RANEFGEVDL NHASSLGGDY MGVHPMGLFW SLKPEKLLTR LLKRDVMNRP FQVQVKLYDL ELIVNNKVAS APKASLTLER WYVAPGVTRI KVREGRLRGA LFLPPGEGLF PGVIDLFGGL GGLLEFRASL LASRGFASLA LAYHNYEDLP RKPEVTDLEY FEEAANFLLR HPKVFGSGVG VVSVCQGVQI GLSMAIYLKQ VTATVLINGT NFPFGIPQVY HGQIHQPLPH SAQLISTNAL GLLELYRTFE TTQVGASQYL FPIEEAQGQF LFIVGEGDKT INSKAHAEQA IGQLKRHGKN NWTLLSYPGA GHLIEPPYSP LCCASTTHDL RLHWGGEVIP HAAAQEHAWK EIQRFLRKHL IPDVTSQL
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Molecular Weight
46.2 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
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Protein Description
BAAT (Bile Acid-CoA:amino acid N-acyltransferase) is an important enzyme involved in the metabolism of bile acids, playing a crucial role in bile acid conjugation and transport. The study of BAAT and its recombinant protein has gained significance due to its implications in various metabolic disorders and liver diseases. Bile acids are essential for the digestion and absorption of dietary fats and fat-soluble vitamins, and disturbances in their metabolism can lead to conditions such as cholestasis, fatty liver disease, and even liver cirrhosis. Researchers have focused on characterizing the BAAT protein to understand its enzymatic activity, substrate specificity, and regulatory mechanisms. The recombinant form of BAAT enables detailed investigations into its functional properties and interactions with other metabolic pathways. Furthermore, understanding BAAT's role in bile acid homeostasis may provide insights into innovative therapeutic strategies for hepatic disorders. The potential to manipulate BAAT activity through gene editing or pharmacological interventions presents exciting avenues for future research, particularly in developing targeted treatments for liver-related diseases and improving overall metabolic health. In summary, the investigation of BAAT and its recombinant protein stands at the intersection of basic biochemistry and clinical application, highlighting the enzyme's significance in maintaining metabolic equilibrium and its potential as a therapeutic target.
