Analytical Data
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Gene name
HADH
- Application
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Alternative Names
HADH;HAD;HAD1;HADHSC;Hydroxyacyl-coenzyme A dehydrogenase. 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
Q16836
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Expression Region
13-314aa
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AA Sequence
SSSSTASA SAKKIIVKHV TVIGGGLMGA GIAQVAAATG HTVVLVDQTE DILAKSKKGI EESLRKVAKK KFAENLKAGD EFVEKTLSTI ATSTDAASVV HSTDLVVEAI VENLKVKNEL FKRLDKFAAE HTIFASNTSS LQITSIANAT TRQDRFAGLH FFNPVPVMKL VEVIKTPMTS QKTFESLVDF SKALGKHPVS CKDTPGFIVN RLLVPYLMEA IRLYERGDAS KEDIDTAMKL GAGYPMGPFE LLDYVGLDTT KFIVDGWHEM DAENPLHQPS PSLNKLVAEN KFGKKTGEGF YKYK
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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
HADH (Hydroxyacyl-CoA dehydrogenase) is an enzyme that plays a crucial role in fatty acid metabolism and energy production within cells. It catalyzes the oxidative conversion of hydroxyacyl-CoA derivatives to ketoacyl-CoA, a key step in the mitochondrial oxidation of fatty acids. Research on HADH is vital due to its implications in various metabolic disorders, including fatty acid oxidation defects and certain forms of obesity, diabetes, and cardiovascular diseases. Abnormal HADH function can lead to the accumulation of toxic intermediates, adversely affecting cellular functions and overall metabolism. Moreover, HADH is a potential therapeutic target for drug development aimed at enhancing mitochondrial function and improving lipid metabolism. Various strategies, including recombinant protein technology, have been employed to produce HADH, facilitating detailed biochemical and structural studies. This research not only enhances our understanding of HADH's role in metabolism but also aids in the development of potential interventions for related metabolic diseases. Understanding the kinetics, structure, and regulation of HADH is essential to harnessing its therapeutic potential, paving the way for innovative treatments in metabolic disease management. As a result, ongoing studies on HADH recombinant protein are critical, offering insights into its functional mechanisms and potential biomedical applications.
