Analytical Data
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Gene name
ACAA2
- Application
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Alternative Names
ACAA2；3-ketoacyl-CoA thiolase. 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
P42765
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Expression Region
17-397aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSFGAYGGLLKDFTATDLSEFAAKAALSA GKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCG SGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIK LEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAA NDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDG TVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMG IGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNV NGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII QSTA
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Molecular Weight
43 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
ACAA2, or Acetyl-CoA acyltransferase 2, is an essential enzyme involved in fatty acid metabolism, specifically in the β-oxidation pathway within the mitochondria. It plays a crucial role in the conversion of fatty acyl-CoA into enoyl-CoA and is critical for maintaining energy homeostasis in cells by facilitating the breakdown of fatty acids. Mutations or deficiencies in ACAA2 can lead to metabolic disorders, including defects in fatty acid oxidation, which are associated with various clinical symptoms such as hypoketotic hypoglycemia and accumulation of long-chain fatty acids. Research on ACAA2 has gained momentum due to its potential implications in understanding metabolic diseases and developing therapeutic strategies. Recombinant ACAA2 protein is increasingly utilized in studies to characterize its enzymatic activity, understand its structure-function relationships, and investigate its interactions with other metabolic pathways. Moreover, advancements in protein expression systems have enabled the production of large quantities of ACAA2 for in vitro studies, allowing researchers to explore its role in cellular metabolism further. Consequently, the exploration of ACAA2 through recombinant protein research holds promise not only for basic metabolic research but also for potential clinical applications in treating metabolic disorders linked to fatty acid oxidation.
