LSD1 | Lesion simulating disease 1 (rabbit antibody)
AS13 2746 | Clonality: Polyclonal | Host: Rabbit | Reactivity: Arabidopsis thaliana

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Product Information
KLH-conjugated synthetic peptide derived from Arabidopsis thaliana LSD1 sequence, UniProt:P94077, TAIR: AT4G20380
20 kD
Reactivity
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Application examples

40 µg of total protein from 0.4g leaves extracted with1ml extraction buffer (50 mM Tris-HCl, pH 6.8, 50mM DTT, 4%SDS, 10%glycerol,PVPP) were separated on12 % SDS-PAGE using tank transfer and blotted 1h to PVDF. Blots were blocked with 5% skimmed milk powder for 1h at room temperature (RT) with agitation. Blot was incubated in the primary antibody at a dilution of 1: 1 000 for 4 h at RT with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at RT with agitation. Blot was incubated in secondary antibody (anti-rabbit IgG horse radish peroxidase conjugated, from ) diluted to 1:0 000 in for 1h at RT with agitation. The blot was washed as above and developed for 5 min with ECL according to the manufacturer's instructions. Exposure time was second.
Courtesy of Dr. Tingting Chai, South China Normal University, China

Reactant: Arabidopsis thaliana (Thale cress)
Application: Western Blotting
Pudmed ID: 25999965
Journal: Front Plant Sci
Figure Number: 3A
Published Date: 2015-05-23
First Author: Chai, T., Zhou, J., et al.
Impact Factor: 5.435
Open PublicationConformation of LSD1 was changed by immunoprecipitation assay and LSD1 activity was indirectly measured under RL. (A) Total protein extracted with (+) or without (–) DTT (50 mM) in the extraction buffer from control, RL, DCMU, and DCMU + RL treated WT was subjected to immunoprecipitation analysis, both dimmer, and monomer LSD1 protein were detected. (B) Total protein was extracted from WT leaves at times after RL treatment and analyzed by an immunoprecipitation assay. (C) The LSD1 conformation was detected in hy5-215 mutant. (D) The ratio of LSD1 dimer/monomer was analyzed quantitatively. (E) The CAT activity was measured in WT, lsd1-2 mutant, and hy5-215 mutant, the four-week old leaves were exposed to control, RL, DCMU and DCMU+ RL for 6 h. (F) The CAT activity of WT, lsd1-2 mutant, and hy5-215 mutant was detected at times after RL treatment. Different letters indicate statistically significant differences between treatments (Duncan's multiple range test: P < 0.05). Values represent means ą SD of three independent replicates.

Reactant: Arabidopsis thaliana (Thale cress)
Application: Western Blotting
Pudmed ID: 25999965
Journal: Front Plant Sci
Figure Number: 3B
Published Date: 2015-05-23
First Author: Chai, T., Zhou, J., et al.
Impact Factor: 5.435
Open PublicationConformation of LSD1 was changed by immunoprecipitation assay and LSD1 activity was indirectly measured under RL. (A) Total protein extracted with (+) or without (–) DTT (50 mM) in the extraction buffer from control, RL, DCMU, and DCMU + RL treated WT was subjected to immunoprecipitation analysis, both dimmer, and monomer LSD1 protein were detected. (B) Total protein was extracted from WT leaves at times after RL treatment and analyzed by an immunoprecipitation assay. (C) The LSD1 conformation was detected in hy5-215 mutant. (D) The ratio of LSD1 dimer/monomer was analyzed quantitatively. (E) The CAT activity was measured in WT, lsd1-2 mutant, and hy5-215 mutant, the four-week old leaves were exposed to control, RL, DCMU and DCMU+ RL for 6 h. (F) The CAT activity of WT, lsd1-2 mutant, and hy5-215 mutant was detected at times after RL treatment. Different letters indicate statistically significant differences between treatments (Duncan's multiple range test: P < 0.05). Values represent means ą SD of three independent replicates.

Reactant: Arabidopsis thaliana (Thale cress)
Application: Western Blotting
Pudmed ID: 25999965
Journal: Front Plant Sci
Figure Number: 3C
Published Date: 2015-05-23
First Author: Chai, T., Zhou, J., et al.
Impact Factor: 5.435
Open PublicationConformation of LSD1 was changed by immunoprecipitation assay and LSD1 activity was indirectly measured under RL. (A) Total protein extracted with (+) or without (–) DTT (50 mM) in the extraction buffer from control, RL, DCMU, and DCMU + RL treated WT was subjected to immunoprecipitation analysis, both dimmer, and monomer LSD1 protein were detected. (B) Total protein was extracted from WT leaves at times after RL treatment and analyzed by an immunoprecipitation assay. (C) The LSD1 conformation was detected in hy5-215 mutant. (D) The ratio of LSD1 dimer/monomer was analyzed quantitatively. (E) The CAT activity was measured in WT, lsd1-2 mutant, and hy5-215 mutant, the four-week old leaves were exposed to control, RL, DCMU and DCMU+ RL for 6 h. (F) The CAT activity of WT, lsd1-2 mutant, and hy5-215 mutant was detected at times after RL treatment. Different letters indicate statistically significant differences between treatments (Duncan's multiple range test: P < 0.05). Values represent means ą SD of three independent replicates.
Additional information
Background
Alternative names: CHILLING SENSITIVE 4, CHS4.
Product citations
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