Analytical Data
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Gene name
HAGHL
- Application
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Alternative Names
HAGHL; Hydroxyacylglutathione hydrolase-like protein; EC 3.1.2.-
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6PII5
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Expression Region
1-203aa
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AA Sequence
MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRVSARSREGRGGRPGSTRPHRSACSSAAVRGHPRALPPDARPHRRPHELLPVGGRLPGPTRPVLGRRAVGGRLRLVPGGQRPADVPEPGRAGYPAPRDEGVLRPRAHA
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Molecular Weight
48.5 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
Related Products
Protein Description
HAGHL (Hydroxyacyl-glutathione hydrolase) is an enzyme that plays a crucial role in the detoxification of aldehydes and harmful metabolites in the human body. The enzyme is part of the glutathione S-transferase family and is involved in the hydrolysis of hydroxyacyl-glutathione conjugates, which are formed during metabolic processes. Research into HAGHL has gained significance due to its potential implications in various diseases, especially those related to oxidative stress and inflammation. Elevated levels of harmful metabolites associated with metabolic disorders can lead to tissue damage and contribute to conditions such as cancer, neurodegenerative diseases, and cardiovascular disorders. Understanding the structure and function of HAGHL at the molecular level can provide insights into its enzymatic activity and regulatory mechanisms. Furthermore, the synthesis and characterization of recombinant HAGHL proteins facilitate studies on enzyme kinetics, substrate specificity, and potential therapeutic applications. The exploration of HAGHL's role in cellular detoxification pathways not only aids in elucidating disease mechanisms but also identifies novel biomarkers for disease diagnosis and prognosis. As research progresses, HAGHL emerges as a promising target for drug development, with the potential to enhance detoxification strategies and mitigate the adverse effects of toxic metabolites in various pathological conditions.
