LOX | Lipoxygenase
AS06 128 | Clonality: Polyclonal | Host: Rabbit | Reactivity: A.thaliana, G. max, L. longiflorum, L. luteus, O. europaea, O. sativa
DATA SHEET IN PDF| Data sheet | Product citations | Protocols | Customer reviews |
Product Information
Immunogen
native lipoxygenase, type I-B, purified from Glycine max (Sigma, product number L7395) UniProt: P08170
Host
Rabbit
Clonality
Polyclonal
Purity
Serum
Format
Lyophilized
Quantity
50 ĩl
Reconstitution
For reconstitution add 50 ĩl of sterile water
Storage
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Tested applications
Western blot (WB)
Recommended dilution
1 : 1000 (WB)
Expected | apparent MW
54 (subunit), 108 (native enzyme)
Reactivity
Confirmed reactivity
Arabidopsis thaliana, Glycine max, Lilium longiflorum, Lupinus luteus, Musa acuminate, Musa paradisiaca L., Nicotiana benthamiana, Olea europaea, Oryza sativa
Predicted reactivity
Glycine max, Lathyrus undulatus, Malus x domestica, Solanum tuberosum, Vicia faba
Species of your interest not listed? Contact us
Not reactive in
Chlamydomonas reinhardtii
Application examples
Application examples
Application example
Samples of Arabidopsis thaliana (2), Olea europaea (3), Lilium Longiflorum (4), Lupinus luteus (5) were ground in liquid nitrogen to a very fine powder using a mortar and pestle and resuspended in 1.5 ml of extraction buffer (4% SDS, 2% 2-mercaptoethanol, 2 mM PMSF, 100 mM Tris-HCl pH 8.5). The samples were incubated for 3 min at 80°C. Protein suspensions were clarified by centrifugation at 13,500 g for 10 min at room temperature and the resulting supernatants were used. Total proteins (25 µg per sample) were separated by SDS-PAGE on CriterionTMTGXTM Precast Gel (Bio-Rad, USA) using CriterionTM Cell apparatus (Bio-Rad). Proteins were electroblotted onto a PVDF membrane using Trans-Blot® TurboTM Transfer Pack (Bio-Rad) in a Trans-Blot® TurboTM Transfer System (Bio-Rad). The membrane was blocked for 1 h in solution containing 1 % (w/v) non-fat dry milk in TRIS-buffered saline (TBS) buffer, pH 7.4. The membrane was incubated in the primary antibody at a dilution of 1: 1000 in TBS buffer containing 1 % (w/v) non-fat dry milk over night at 4°C with agitation. A DyLight 488 conjugated anti-rabbit IgG (AS10 831, Agrisera), diluted 1:2000 in TBS buffer for 2 h, served as the secondary antibody. The signal was detected in a Pharos FX molecular imager (Bio-Rad). Line 1 contains LOX protein from Sigma.
Courtesy of Dr. Agnieszka Zienkiewicz, CSIC, Spain
Samples of Arabidopsis thaliana (2), Olea europaea (3), Lilium Longiflorum (4), Lupinus luteus (5) were ground in liquid nitrogen to a very fine powder using a mortar and pestle and resuspended in 1.5 ml of extraction buffer (4% SDS, 2% 2-mercaptoethanol, 2 mM PMSF, 100 mM Tris-HCl pH 8.5). The samples were incubated for 3 min at 80°C. Protein suspensions were clarified by centrifugation at 13,500 g for 10 min at room temperature and the resulting supernatants were used. Total proteins (25 µg per sample) were separated by SDS-PAGE on CriterionTMTGXTM Precast Gel (Bio-Rad, USA) using CriterionTM Cell apparatus (Bio-Rad). Proteins were electroblotted onto a PVDF membrane using Trans-Blot® TurboTM Transfer Pack (Bio-Rad) in a Trans-Blot® TurboTM Transfer System (Bio-Rad). The membrane was blocked for 1 h in solution containing 1 % (w/v) non-fat dry milk in TRIS-buffered saline (TBS) buffer, pH 7.4. The membrane was incubated in the primary antibody at a dilution of 1: 1000 in TBS buffer containing 1 % (w/v) non-fat dry milk over night at 4°C with agitation. A DyLight 488 conjugated anti-rabbit IgG (AS10 831, Agrisera), diluted 1:2000 in TBS buffer for 2 h, served as the secondary antibody. The signal was detected in a Pharos FX molecular imager (Bio-Rad). Line 1 contains LOX protein from Sigma.
Courtesy of Dr. Agnieszka Zienkiewicz, CSIC, Spain
Additional information
Background
Background
Lipoxygenases (LOXs; EC 1.13.11.12, synonym: lipoxydases) are a family of enzymes that catalyze oxygenation of polyunsaturated fatty acids (PUFAs) into lipidhydroperoxides (LOOHs) involved in responses to stresses. LOXs has been found to play a role in plant growth and development, senescence as well as can be activated in response to environamental stress (drought, heavy metals). Synonymes: linoleate, oxygen oxidoreductase.
Product citations
Selected references
Kucko et al. (2022) The acceleration of yellow lupine flower abscission by jasmonates is accompanied by lipid-related events in abscission zone cells, Plant Science, Volume 316, 2022,111173, ISSN 0168-9452, https://doi.org/10.1016/j.plantsci.2021.111173. (https://www.sciencedirect.com/science/article/pii/S0168945221003691)
Zhu et al. (2021) Physiological and Proteomic Analyses Reveal Effects of Putrescine-Alleviated Aluminum Toxicity in Rice Roots[J]. RICE SCI, 0, (): 3-.
Castro et al. (2020). Identification of seed storage proteins as the major constituents of the extra virgin olive oil proteome. Food Chem X . 2020 Jun 27;7:100099.doi: 10.1016/j.fochx.2020.100099.
Yang et al. (2012). Quantitative proteomic analysis reveals that antioxidation mechanisms contribute to cold tolerance in plantain (Musa paradisiaca L.; ABB Group) seedlings. Mol Cell Proteomics. 2012 Dec;11(12):1853-69. doi: 10.1074/mcp.M112.022079.
Huang et al. (2011). Cloning and characterization of a 9-lipoxygenase gene induced by pathogen attack from Nicotiana benthamiana for biotechnological application. BMC Biotechnol. 2011 Mar 30;11:30. doi: 10.1186/1472-6750-11-30.
Huang et al. (2010). Overexpression of hydroperoxide lyase gene in Nicotiana benthamiana using a viral vector system. Plant Biotechnol J. 2010 Sep;8(7):783-95. doi: 10.1111/j.1467-7652.2010.00508.x.
Zhu et al. (2021) Physiological and Proteomic Analyses Reveal Effects of Putrescine-Alleviated Aluminum Toxicity in Rice Roots[J]. RICE SCI, 0, (): 3-.
Castro et al. (2020). Identification of seed storage proteins as the major constituents of the extra virgin olive oil proteome. Food Chem X . 2020 Jun 27;7:100099.doi: 10.1016/j.fochx.2020.100099.
Yang et al. (2012). Quantitative proteomic analysis reveals that antioxidation mechanisms contribute to cold tolerance in plantain (Musa paradisiaca L.; ABB Group) seedlings. Mol Cell Proteomics. 2012 Dec;11(12):1853-69. doi: 10.1074/mcp.M112.022079.
Huang et al. (2011). Cloning and characterization of a 9-lipoxygenase gene induced by pathogen attack from Nicotiana benthamiana for biotechnological application. BMC Biotechnol. 2011 Mar 30;11:30. doi: 10.1186/1472-6750-11-30.
Huang et al. (2010). Overexpression of hydroperoxide lyase gene in Nicotiana benthamiana using a viral vector system. Plant Biotechnol J. 2010 Sep;8(7):783-95. doi: 10.1111/j.1467-7652.2010.00508.x.
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