Analytical Data
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Gene name
EHHADH
- Application
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Alternative Names
3 hydroxyacyl CoA dehydrogenase; 3,2 trans enoyl CoA isomerase; 3-hydroxyacyl-CoA dehydrogenase; ECHD; ECHP_HUMAN; EHHADH; Enoyl Coenzyme A; Enoyl Coenzyme A; hydratase/3 hydroxyacyl Coenzyme A dehydrogenase ; L 3 hydroxyacyl CoA dehydrogenase; L bifunctional protein; L bifunctional protein; peroxisomal; L PBE; LBFP; LBP; MGC120586; MS730; PBE; PBFE; Peroxisomal bifunctional enzyme; Peroxisomal enoyl CoA hydratase
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08426
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Expression Region
1-723aa
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Molecular Weight
95.5 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
EHHADH (Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase) is a key enzyme involved in the beta-oxidation of fatty acids and plays a significant role in lipid metabolism. Dysregulation of EHHADH has been implicated in various metabolic disorders, including obesity, diabetes, and cardiovascular diseases. The study of EHHADH recombinant proteins has gained attention due to the enzyme's potential as a therapeutic target and its utility in understanding fatty acid catabolism. By producing recombinant EHHADH, researchers aim to elucidate its structure-function relationships and explore the mechanisms by which it contributes to metabolic balance. Insights gained from recombinant EHHADH studies may lead to novel interventions for metabolic diseases and improve our understanding of energy homeostasis in the body. Furthermore, advances in protein engineering and purification techniques facilitate the detailed characterization of EHHADH, allowing for the exploration of its regulatory pathways and the identification of inhibitors or activators that could be developed into pharmacological agents. As obesity and metabolic syndrome continue to be pressing global health issues, EHHADH stands out as a promising candidate for further research aimed at enhancing metabolic health and developing targeted therapies.
