Analytical Data
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Gene name
Leukotriene A4 Hydrolase/LTA4H
- Application
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Alternative Names
LTA4 Hydrolase
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P24527
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Expression Region
Gln135~Glu272
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Molecular Weight
19kDa
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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
Leukotriene A4 hydrolase (LTA4H) is a crucial enzyme in the leukotriene biosynthesis pathway, catalyzing the conversion of leukotriene A4 (LTA4) to leukotriene B4 (LTB4), a potent pro-inflammatory mediator involved in various immune responses. Dysregulation of LTA4H and leukotriene signaling has been implicated in numerous inflammatory diseases, including asthma, rheumatoid arthritis, and cardiovascular disorders. The study of recombinant LTA4H protein has gained significance in understanding its enzymatic mechanisms, regulatory functions, and potential as a therapeutic target. Recombinant expression systems allow for the production of LTA4H in sufficient quantities for detailed biochemical and structural analyses. Researchers aim to elucidate the substrate specificity, kinetic parameters, and structural characteristics of LTA4H using techniques such as X-ray crystallography and enzyme assays. Furthermore, investigating LTA4H inhibitors can provide insights into novel anti-inflammatory strategies. Understanding the functional dynamics of LTA4H not only contributes to the fundamental knowledge of leukotriene metabolism but also paves the way for developing targeted therapies aimed at modulating inflammation and treating related diseases.
