Analytical Data
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Gene name
ACOT7
- Application
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Alternative Names
ACOT7；BACH；Cytosolic acyl coenzyme A thioester hydrolase
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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
O00154
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Expression Region
1-370aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MARPGLIHSA PGLPDTCALL QPPAASAAAA PSMSGPDVET PSAIQICRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP
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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
Related Products
Protein Description
ACOT7 (Acyl-CoA Thioesterase 7) is a member of the acyl-CoA thioesterase family, which plays a crucial role in fatty acid metabolism by hydrolyzing acyl-CoA esters into free fatty acids and CoA. This enzymatic activity is fundamental for various cellular processes, including energy production, lipid signaling, and the regulation of metabolic pathways. Alterations in ACOT7 expression have been implicated in several diseases, including obesity, diabetes, and cancer, highlighting its potential as a therapeutic target. Recent studies have focused on understanding the structural and functional characteristics of ACOT7, emphasizing its potential role in modulating lipid homeostasis and its involvement in metabolic diseases. The recombinant production of ACOT7 allows for a detailed investigation of its enzymatic properties and interactions with different acyl-CoA substrates. By utilizing advanced techniques in protein expression and purification, researchers aim to elucidate the mechanisms through which ACOT7 regulates lipid metabolism and its impact on cellular health. Additionally, understanding its functional dynamics may pave the way for developing novel therapeutic approaches to target metabolic disorders linked to aberrant fatty acid metabolism. This research is essential for advancing our knowledge of lipid biology and offers promising avenues for biomedical applications in treating metabolic diseases.
