Analytical Data
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Gene name
ECH1
- Application
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Alternative Names
HPXEL; 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
N-His
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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
Met1~Leu328
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Molecular Weight
40kDa
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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 (enoyl-CoA hydratase 1) is an essential enzyme in the mitochondrial fatty acid β-oxidation pathway, playing a crucial role in the catabolism of medium- and long-chain fatty acids. Deficiencies in ECH1 have been linked to various metabolic disorders, including very-long-chain acyl-CoA dehydrogenase deficiency (VLCADD) and other fatty acid oxidation-related pathologies. The study of ECH1 recombinant protein is vital for further understanding its structure-function relationships and the underlying mechanisms of its activity. Recent advances in recombinant DNA technology have enabled the expression of ECH1 in heterologous systems, facilitating the purification and characterization of the protein. Researchers are particularly interested in elucidating the enzyme's kinetic properties, substrate specificity, and interaction with cofactors, which are crucial for its catalytic function. Additionally, investigating the impact of mutations on ECH1's activity could provide insights into the pathophysiology of related metabolic disorders. Such studies not only contribute to the fundamental knowledge of lipid metabolism but also have potential therapeutic implications, paving the way for the development of targeted treatments for conditions associated with ECH1 dysfunction. Overall, the research on ECH1 recombinant protein serves as a vital bridge connecting molecular biology and clinical applications, with the potential to improve diagnosis and treatment strategies for metabolic diseases.
