Analytical Data
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Gene name
ALOX15
- Application
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Alternative Names
LOX15; 15-LOX2; 15-LOX1; 15-LOX; 12-LOX; ALOX15; 15-LO; 15-LPG; LOG15; Lipoxygenase 15; Arachidonate 12-lipoxygenase, leukocyte-type; Arachidonate omega-6 lipoxygenase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16050
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Expression Region
Lys170~Leu312
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Molecular Weight
17kDa
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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
The ALOX15 gene encodes a lipoxygenase enzyme that plays a critical role in the metabolism of polyunsaturated fatty acids, leading to the production of bioactive lipid mediators involved in various physiological and pathological processes, including inflammation, cell proliferation, and apoptosis. Research on ALOX15 has garnered attention due to its potential implications in diseases such as asthma, cancer, and cardiovascular disorders. The enzyme catalyzes the conversion of arachidonic acid and other fatty acids into leukotrienes and hydroxyeicosatetraenoic acids, which are vital in modulating immune responses. Given the increasing interest in the therapeutic potential of targeting lipoxygenase pathways, the production of recombinant ALOX15 protein has become a crucial focus. This recombinant protein facilitates detailed biochemical and biophysical studies, enabling researchers to investigate the structure-function relationship of the enzyme and its metabolic pathways. Understanding ALOX15's activity and regulation can provide insights into its role in disease mechanisms and lead to the development of novel therapeutic strategies aimed at modulating its activity. Such research could potentially result in innovative approaches to manage conditions associated with dysregulated arachidonic acid metabolism, highlighting the importance of ALOX15 in both health and disease.
