Analytical Data
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Gene name
aMACR
- Application
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Alternative Names
RACE; 2-methylacyl-CoA racemase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UHK6
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Expression Region
Ala2~Asn148
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Molecular Weight
20kDa
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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
The study of aMACR (alpha-methylacyl-CoA racemase) recombinant protein is rooted in its significant role in the metabolism of branched-chain fatty acids and its implications in various diseases. aMACR is an enzyme that catalyzes the racemization of alpha-methylacyl-CoA esters, an important step in the catabolism of specific fatty acids, particularly those derived from dietary sources. Mutations in the ACOX1 gene, which encodes aMACR, have been linked to disorders in fatty acid metabolism, such as adrenoleukodystrophy and certain types of cancer. Understanding aMACR's functional mechanisms and its regulation can provide insights into metabolic pathways that are crucial for energy production and the synthesis of bioactive lipids. Moreover, research on the recombinant form of this enzyme has allowed for the detailed investigation of its kinetic properties and structural characteristics, paving the way for potential therapeutic applications and the development of novel biomarkers for disease diagnosis. As such, the exploration of aMACR and its recombinant protein serves as a critical focal point for advancing metabolic biology and understanding the intricacies of lipid metabolism in health and disease.
