Analytical Data
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Gene name
Acaca
- Application
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Alternative Names
Acaca;ACAC;ACC1;ACCA;Acetyl-CoA carboxylase 1
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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
Q13085
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Expression Region
78-617aa
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AA Sequence
SMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEKVLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPGGPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMYGVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLETESFQMNRIDTGWLDRLI
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Molecular Weight
67.1 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
Acaca, or Acetyl-CoA carboxylase alpha, is a key enzyme involved in fatty acid metabolism, playing a crucial role in regulating lipid synthesis and energy homeostasis. Recent studies have highlighted its significance in various metabolic disorders, including obesity, type 2 diabetes, and cardiovascular diseases. The enzyme catalyzes the conversion of acetyl-CoA to malonyl-CoA, a critical precursor in fatty acid biosynthesis, thus influencing cellular energy balance and overall metabolic health. Given its pivotal role, understanding the mechanistic aspects of Acaca, including its structure and function, is essential for developing targeted therapies for metabolic diseases. Research into recombinant forms of Acaca has enabled scientists to investigate its enzymatic activity, regulation, and interaction with various ligands, thereby providing insights into its biological significance. Furthermore, the reconstitution of Acaca into lipid biosynthesis pathways in vitro has enhanced our understanding of its regulatory mechanisms and potential as a therapeutic target. Advances in protein engineering and biophysical characterization techniques have facilitated detailed studies on Acaca, paving the way for exploring its potential in drug development and metabolic health interventions. As obesity rates continue to rise globally, the need for effective treatments that target metabolic disorders makes the study of Acaca and its recombinant forms highly relevant in the field of medicinal chemistry and metabolic research. Such insights not only contribute to our fundamental understanding of lipid metabolism but also hold promise for innovative therapeutic strategies aimed at combating the growing epidemic of metabolic diseases.











