Analytical Data
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Gene name
ACAA1
- Application
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Alternative Names
ACAA1；ACAA；PTHIO；3-ketoacyl-CoA thiolase. peroxisomal
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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
P09110
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Expression Region
27-424aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMLSGAPQASAADVVVVHGRRTAICRAGRGG FKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQ FLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSL ADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALA SQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTME GLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLR SYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYC VEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVV SMCIGTGMGAAAVFEYPGN
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Molecular Weight
44 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
ACAA1, or Acetyl-CoA Acyltransferase 1, plays a crucial role in fatty acid metabolism, particularly in the final steps of mitochondrial fatty acid oxidation. This enzyme catalyzes the conversion of 3-ketoacyl-CoA to acetyl-CoA and acyl-CoA, which are vital intermediates in energy production. Research has shown that ACAA1 is essential for maintaining cellular energy homeostasis and regulating lipid metabolism. Mutations or dysregulation of ACAA1 have been implicated in various metabolic disorders, including mitochondrial diseases and obesity-related conditions. Understanding the structure and function of the ACAA1 recombinant protein provides insights into its enzymatic mechanisms and potential therapeutic applications. Recent studies focus on characterizing the recombinant form of ACAA1 through techniques such as crystallography and enzymatic assays, aiming to elucidate its catalytic properties and interaction with cofactors. These investigations not only enhance our understanding of fatty acid metabolism but also pave the way for developing targeted treatments for metabolic diseases associated with ACAA1 dysfunction. As a result, ACAA1 has gained significant interest in biochemical research, highlighting its potential as a biomarker and target for drug development.
