Cat | Catalase (peroxisomal marker)

Western blot analysis of antioxidant enzymes in purified mitochondria from 0 d, 3 d, and 4 d aged seeds.Total 10 ?g protein was separated by SDS gel electrophoresis and blotted to supported polyvinylidene difluoride, then probed with antibodies against catalase (CAT), glutathione reductase (GR) and manganese superoxide dismutase (MnSOD).

Detection of superoxide dismutase 1 (SOD1) and catalase (CAT) using western blotting for the control (C), antioxidant (AO; 400 µg/ml ascorbic acid and 200 µg/ml cysteine), 1 mM H2O2 reactive oxygen species (ROS), and AO + ROS treatment groups. Immunoprobing for SOD1 and CAT (a). SOD1 mean protein band intensities for window stage (b) and mature leaves (c). CAT mean protein band intensities for window stage (d) and mature leaves (e). One-way ANOVA, Dunnett’s multiple comparison test, **P < 0.01; *P < 0.05 ns, non-significant; n ? 4. Error bars represent standard error

Molecular and biochemical characterizations of the catalase mutants. a Structures of the CAT1, CAT2 and CAT3 genes are shown with the T-DNA insertion sites in cat1-1 (SAIL_525_C10), cat1-3 (SALK_208924), cat2-2 (SALK_057998), cat2-3 (SALK_144919), cat3-1 (SALK_092911) and cat3-2 (SALK_088601). Exons are indicated by black blocks, introns by solid lines and untranslated regions by grey broken lines. The black arrowhead indicates the orientation of the T-DNA insertion. b Quantitative RT-PCR analysis of CAT gene expressions in wild-type and catalase mutants is shown. Each value for real-time PCR is the mean?±?SE of three independent experiments. c Protein gel blot analysis was performed using anti-catalase serum and total proteins were extracted from seeds grown under 16-h light/8-h dark conditions for 24 h after stratification. Protein extracts were stained with Ponceau S as a loading control. The protein gel blot assay was repeated independently three times. d The effect of 3-AT on seed germination in catalase mutants. Germination rates were recorded for the wild-type, CAT homozygous mutants grown under light conditions (16 h light/8 h dark) for 60 h after stratification on MS medium supplemented with 0, 5mM 3-AT. Each value is the mean?±?SE of three independent biological experiments, and different letters indicate significant differences at P?<?0.05 (Duncan’s multiple range test) when comparing values within the same 3-AT concentration

Expression analysis of CAT members in the seeds of Col-0, ABI5OE-Myc and abi5-1. The seeds of Col-0, ABI5OE-Myc and abi5-1 were grown under 16-h light/8-h dark conditions for 24 h after stratification on MS medium supplemented with 0 or 5mM 3-AT. a–c are quantitative RT-PCR analysis of CAT1 (A), CAT2 (B) and CAT3 (C), respectively. Each value is the mean?±?SE of three independent experiments. d Protein gel blot analysis of the expression of CAT in the seeds of Col-0, ABI5OE-Myc and abi5-1. Protein extracts were stained with the Ponceau S as a loading control. The assay was independently repeated three times

Accumulation of BiP, Catalase, and ATP synthase (beta chain) by western blot and analysis of spots. a Image of a nitrocellulose membrane hybridized with Anti-BiP, Anti-Catalase, and Anti-ATP synthase (beta chain) of Arabidopsis (Normalization, see Additional file 6: Figure S4). b Relative accumulation determined from images of the nitrocellulose membrane, using the Gel Quant. Net 1.8.0 software. c Relative quantification of each spot corresponding to proteins analyzed by western blot. The average values of the each spot’s percentage volume in each gel replicate was used for graph construction

SnRK2.4 and SnRK2.10 modulate catalase (CAT) on multiple levels during response to salt stress. Wild type and snrk2 mutants’ seedlings were subjected to treatment with 150 mM NaCl for times indicated. CAT1 expression was determined by RT-qPCR (A), total catalase protein was determined by immunoblot analysis (B), and total catalase activity assay was performed (C); error bars represent SD; stars represent statistically significant differences in comparison with the wt plants (Student t-test) where * p < 0.05; ** p < 0.001; *** p < 0.0001. After exposure, membranes were stripped and reused for glyceraldehyde 3-phosphate dehydrogenase (GAPDH) detection as a loading control. At least two independent biological replicates of the experiment were performed, each with four samples per data point. Results of one representative experiment are shown.

Catalases (CAT) activity in Arabidopsis grown in vitro, measured 10 days after treatment with BASTA applied at two concentrations B5 (5 mg L?1) and B10 (10 mg L?1), N. rtanjensis essential oil applied at two concentrations 2% (2NrEO) and 4% (4NrEO), and of their combinations. (A,B) CAT activity stain after native-PAGE separation (5 µg per lane of total protein), in shoots and roots, respectively. The detected activities were measured densitometrically and presented as relative CAT activity (% of control) in comparison to non-treated plants (nt). (C,D) CAT immunoblot (20 µg of soluble proteins per line) in shoots and roots, respectively. Heat-maps show relative abundances of CAT proteins. Maximal values on the color scales represent maximal values recorded for each immunoblot.