Analytical Data
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Gene name
ECH1
- Application
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Alternative Names
ECH1；Delta(3.5)-Delta(2.4)-dienoyl-CoA isomerase. 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
Q13011
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Expression Region
34-328aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTGSSAQEAASGVALGEAPDHSYESLRVTS AQKHVLHVQLNRPNKRNAMNKVFWREMVECFNKISRDADCRAVVISGAGK MFTAGIDLMDMASDILQPKGDDVARISWYLRDIITRYQETFNVIERCPKP VIAAVHGGCIGGGVDLVTACDIRYCAQDAFFQVKEVDVGLAADVGTLQRL PKVIGNQSLVNELAFTARKMMADEALGSGLVSRVFPDKEVMLDAALALAA EISSKSPVAVQSTKVNLLYSRDHSVAESLNYVASWNMSMLQTQDLVKSVQ ATTENKELKTVTFSKL
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Molecular Weight
34 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
ECH1, or Enoyl-CoA hydratase 1, is a crucial enzyme in the fatty acid metabolism pathway, particularly involved in the breakdown of fatty acids via the mitochondrial beta-oxidation process. This enzyme facilitates the hydration of enoyl-CoA substrates to form 3-hydroxyacyl-CoA, which is an essential step for the subsequent oxidative reactions that yield energy. Alterations in ECH1 activity have been linked to various metabolic disorders, including obesity, diabetes, and cardiovascular diseases, underscoring its importance in maintaining metabolic homeostasis. Recent studies have focused on the recombinant expression of ECH1 to better understand its structural and functional properties. By producing ECH1 in heterologous systems, researchers aim to characterize its enzymatic activity, investigate its regulation, and explore potential therapeutic targets that could alleviate metabolic dysfunctions. Furthermore, recombinant ECH1 can serve as a valuable tool for high-throughput screening of small molecules that could modulate its activity, paving the way for the development of new strategies in treating metabolic diseases. The study of ECH1 thus not only enhances our understanding of fatty acid metabolism but also holds promise for innovative therapeutic interventions in metabolic health.
