

| Catalog No. | HT104014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Species reactivity | Human | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human ALOX15B (Ala2-Gly121). | ||||||||
| Target | 15-lipoxygenase 2, 15-LOX-B, 15-LOX-2, Linoleate 13-lipoxygenase 15-LOb, Arachidonate 15-lipoxygenase B, Polyunsaturated fatty acid lipoxygenase ALOX15B, ALOX15B, Arachidonate 15-lipoxygenase type II | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | O15296 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Polyunsaturated fatty acid lipoxygenase ALOX15B is a ~75 kDa protein. Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids (PUFAs) generating a spectrum of bioactive lipid mediators (Probable). It inserts peroxyl groups at C15 of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) producing (15S)-hydroperoxyeicosatetraenoate/(15S)-HPETE (Probable). Also peroxidizes linoleate ((9Z,12Z)-octadecadienoate) to 13-hydroperoxyoctadecadienoate/13-HPODE (Probable). Oxygenates arachidonyl derivatives such as 2-arachidonoylglycerol (2-AG) leading to the production and extracellular release of 15-hydroxyeicosatetraenoyl glycerol (15-HETE-G) that acts as a peroxisome proliferator-activated receptor alpha agonist. Has the ability to efficiently class-switch ALOX5 pro-inflammatory mediators into anti-inflammatory intermediates. 1. Kilty, I. et al. (1999) European journal of biochemistry 266, 83-93. PMID: 10542053 2. Jisaka, M. et al. (2000) The Journal of biological chemistry 275, 1287-93. PMID: 10625675 3. Bhatia, B. et al. (2003) The Journal of biological chemistry 278, 25091-100. PMID: 12704195 4. Prusakiewicz, JJ. et al. (2007) Archives of biochemistry and biophysics 464, 260-8. PMID: 17493578 5. Turman, MV. et al. (2008) Biochemistry 47, 3917-25. PMID: 18311922 6. Horn, T. et al. (2013) Redox biology 1, 566-77. PMID: 24282679 7. Kobe, MJ. et al. (2014) The Journal of biological chemistry 289, 8562-9. PMID: 24497644 8. Perry, SC. et al. (2020) Journal of lipid research 61, 1087-1103. PMID: 32404334 9. Brash, AR. et al. (1997) Proceedings of the National Academy of Sciences of the United States of America 94, 6148-52. PMID: 9177185 | ||||||||
| Note | For research use only. |



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