Analytical Data
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Gene name
HAGH
- Application
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Alternative Names
HAGH;GLO2;HAGH1;Hydroxyacylglutathione hydrolase. 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
Q16775
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Expression Region
50-308aa
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AA Sequence
KVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRREKDQFKMPRD
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Molecular Weight
55.7kDa
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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
HAGH (Hydroxyacyl-CoA dehydrogenase) is a key enzyme involved in the metabolism of fatty acids and plays a crucial role in cellular energy production. Its importance extends to various physiological processes, including lipid metabolism and energy homeostasis. Research into HAGH recombinant proteins has gained traction in recent years due to their potential applications in biotechnology and medicine. The ability to produce HAGH in a recombinant form allows for the detailed study of its enzymatic activity, regulation, and structure-function relationships. Understanding the molecular mechanisms by which HAGH operates can provide insights into metabolic disorders linked to fatty acid metabolism, such as obesity and diabetes. Moreover, recombinant HAGH can be utilized in synthetic biology applications, where engineered metabolic pathways are designed to optimize the production of biofuels and other valuable biochemicals. As a result, the exploration of HAGH's recombinant protein holds promise not only for advancing basic biochemical knowledge but also for developing innovative solutions to address metabolic diseases and enhance the efficiency of industrial processes. This research is underscored by the increasing demand for sustainable energy sources and the need for therapeutic targets in metabolic regulation, marking HAGH as a significant focus in current scientific inquiries.
