The list of the primary and secondary antibodies and their dilutions is given in Table 1 . Superoxide dismutase, Anti-Catalase, Anti-Glutathione Reductase from Abcam (Cambridge, MA, USA), while FITC, 1:1000 and TRITC were bought from Jackson ImmunoResearch Laboratories (Ely, Cambridgeshire, UK).
Anti catalase
Manufactured by Abcam
Sourced in United States, United Kingdom
Anti-catalase is a laboratory reagent used for the detection and quantification of catalase, an enzyme that plays a crucial role in the breakdown of hydrogen peroxide. This product can be used to measure catalase activity in various biological samples.
Automatically generated - may contain errors
Lab products found in correlation
Anti akt, by Cell Signaling Technology (2 mentions)
Anti gapdh, by Santa Cruz Biotechnology (2 mentions)
Anti jak2, by Cell Signaling Technology (2 mentions)
Anti actin, by Merck Group (2 mentions)
Anti cleaved caspase 3, by Cell Signaling Technology (2 mentions)
N acetyl l cysteine, by Merck Group (2 mentions)
Anti gapdh, by Abcam (2 mentions)
Anti β actin, by Merck Group (2 mentions)
Anti pex5, by GeneTex (2 mentions)
Anti lc3, by Merck Group (2 mentions)
Anti bax, by Cell Signaling Technology (2 mentions)
Anti β actin, by Cell Signaling Technology (2 mentions)
Anti gapdh, by Cell Signaling Technology (2 mentions)
Anti β actin, by Abcam (2 mentions)
Anti sod2, by Abcam (2 mentions)
Fluorescein isothiocyanate (fitc), by Jackson ImmunoResearch (1 mentions)
Superoxide dismutase, by Abcam (1 mentions)
Anti pser473 akt, by Cell Signaling Technology (1 mentions)
Annexin 5 pe apoptosis detection kit, by Thermo Fisher Scientific (1 mentions)
Anti mtor, by Cell Signaling Technology (1 mentions)
23 protocols using anti catalase
1
Antioxidant Enzyme Immunostaining Protocol
2
Erythroid Precursor Analysis in Bone Marrow and Spleen
3
Detailed Antibody Panel for Signaling Assays
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The antibodies used in the study: mouse monoclonal anti-phosphotyrosine antibody (catalog 05–321, clone 4G10; Millipore); anti-pY1162/1163-IR-β (catalog 700393, clone 97H9L7; Invitrogen); anti-IR-β (catalog sc-711, clone C711; Santa Cruz Biotechnology Inc.); anti-actin (catalog A2228, clone AC-74, Sigma-Aldrich); anti-p-T308 AKT (catalog 13038, clone D25E6; Cell Signaling Tech), anti-AKT (catalog 4691, clone C67E7; Cell Signaling Tech), anti-JAK2 (catalog 3230, clone D2E12; Cell Signaling Tech); anti-catalase (catalog ab16731; abcam), anti-HA (catalog 11583816001, clone 12CA5; Roche), and anti-PTP1B (EP1841Y; abcam). Antibodies were used at dilutions recommended by the manufacturers.
4
TRAIL-induced Apoptosis Pathway
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SC F2 was kindly provided by Gangneung-Wonju National University [17 (link)]. Drug treatments were performed by inhaling the medium and replacing it with drugs containing medium. TRAIL protein (recombinant human) was purchased from Millipore (Millipore, Darmstadt, Germany). Protein G PLUS-agarose, anti-Bcl-2, anti-Bax, anti-Ub, anti-SOD 3, anti-DR5, anti-DR4 and anti-Bcl-xL were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Anti-Mcl-1, anti-XIAP, anti-cleaved caspase-9, anti-cleaved caspase-8, anti-cleaved caspase-3, anti-Noxa, anti-Puma, anti-Bim, anti-Survivin, anti-p-JNK, anti-JNK, anti-CHOP, anti-PERK, anti-p-PERK, anti-ATF6, anti-IRE-1α, anti-ATF4, anti-eIF2a, anti-p-eIF2a, anti-GRP78, anti-GRP94, anti-SOD 1, anti-SOD 2 and anti-PARP-1 were purchased from Cell Signaling Technology (Beverly, MA, USA). Anti-p-IRE-1α and anti-catalase were purchased from Abcam (Cambridge, England). Anti-actin, DCFH-DA, N-acetyl L-cysteine (NAC) and H2O2 were purchased from Sigma (Sigma, St. Louis, MO, USA).
5
Western Blot Analysis of Antioxidant Enzymes
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Protein expression manganese superoxide dismutase (Mn-SOD), catalase (CAT) and glutathione peroxidase (GSH-Px-1) was determined by Western blot with specific antibodies (anti-Mn-SOD, Millipore, 06-984, Darmstadt, Germany 1/1000 dilution; anti-Catalase, Abcam Laboratories, ab1877, Cambridge, UK, 1/10000 dilution and anti-GSH-Px-1, Abcam Laboratories, ab22604, Cambridge, UK, 1/1000 dilution respectively) as described elsewhere [90 (link)], the secondary anti-rabbit antibody (IC-3R01; 1:1000; Imuny Rheabiotech, SP, Brazil). The signals obtained on immunoblot determinations were scanned and quantified by densitometric analysis with a chemoluminescence detection device (Odyssey Imaging System, Li-Cor Biosciences, Lincoln, NE, USA).
All protein expression bands obtained by Western blotting were analyzed with Image J Software version 1.46a (NIH, Bethesda, MD, USA) and the integrate density values were normalized by the loading control band (α-tubulin: #3873; 1:500; Cell Signaling, Inc., Danvers, MA, USA).
All protein expression bands obtained by Western blotting were analyzed with Image J Software version 1.46a (NIH, Bethesda, MD, USA) and the integrate density values were normalized by the loading control band (α-tubulin: #3873; 1:500; Cell Signaling, Inc., Danvers, MA, USA).
6
Glyceraldehyde Oxidative Stress Assay
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Glyceraldehyde (GA; catalog number: 17014-81) was purchased from Nacalai Tesque (Kyoto, Japan). N-acetyl-L-cysteine (NAC; catalog number: A9165) and 3-amino-1,2,4-triazole (3-AT; catalog number: A8056) were obtained from Sigma-Aldrich (St. Louis, MI, USA). Aminoguanidine (AG; catalog number: 328-26432) and hydrogen peroxide (H2O2; catalog number: 081-04215) were from FUJIFILM Wako Pure Chemical Corporation (Osaka, Japan). The following antibodies were used in the present study: anti-catalase (Abcam, Cambridge, UK, catalog number: ab209211) and anti-β-tubulin antibodies (FUJIFILM Wako Pure Chemical Corporation, catalog number: 014-25041). An anti-TAGE antibody was prepared and purified as described previously [45 (link)].
7
Osteoblast Protein Expression Analysis
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Total proteins were extracted from HOB and MC3 T3‐E1 cells, the primary osteoblasts isolated from the bone tissues of patients with osteoporosis and osteoarthritis or the osteoblasts isolated from the mouse bone marrow. The protein concentrations were tested using the BCA Protein Assay Kit (Beyotime). In total, 30 μg of protein from each sample was applied for SDS‐PAGE. After separation, the proteins were transferred into PVDF membranes (Roche, Basel, Switzerland). The PVDF membranes were blocked for nearly 1 h and then incubated with the primary antibodies anti‐FOXO3a (Abcam, 1/2500), anti‐TRIM33 (Abcam, 1/1000), anti‐Lamin B (Abcam, 1/2000), anti‐GAPDH (Abcam, 1/2500), anti‐CBP (Abcam, 1/1000), anti‐Gadd45a (Abcam, 1/1000), anti‐FOXO1 (Abcam, 1/2000), anti‐FOXO4 (Abcam, 1/2000) and anti‐catalase (Abcam, 1/2000) at 4°C for about 24 h. This was followed by the incubation with the corresponding secondary antibodies (Abcam, 1/2000) at room temperature for nearly 1 h. Protein bands were visualized using BeyoECL Moon (Beyotime). LaminB and GAPDH were applied as the references for nuclear protein and total protein, respectively.
8
Mitochondrial Protein Validation by Western Blot
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Western blot analysis was performed to validate the levels of protein expression changes identified in the proteomics profiling. 20 µg samples of the mitochondrial fractions from each sample were resolved employing the same protocol described above. Three primary antibodies were used: rabbit polyclonal HSP60 (Santa Cruz Biotechnology, Inc, sc13966), rabbit polyclonal anti-Catalase (Abcam, Cambridge, USA; ab16731) and rabbit polyclonal NDUFS1 (Abcam, Cambridge, USA; ab96428). Rabbit polyclonal anti-VDAC was used as a loading control. After incubating with the respective secondary antibodies (anti-rabbit), bands were visualized by enhanced chemiluminescence and exposed to film. The band intensities were measured using ImageJ software (http://rsbweb.nih.gov/ij/ ).
9
Amyloid-β Peptide Aggregation Assay
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The Aβ42 peptides were prepared as described previously. We incubate Aβ (100 μM)/E22K and catalase (80 μM) for one hour at room temperature. Then, coincubated solutions of Aβ/catalase and E22K/catalase were dissolved in sample buffer (8 M urea, 100 mM tricine, 8% sodium dodecyl sulfate (SDS), 30% glycerol, 0.01% phenol red, and 10% mercaptoethanol). The proteins were electrophoretically separated by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and then transferred to polyvinylidene fluoride (PVDF) membranes (0.2 mM pore size, Bio-Rad). The membranes were blocked in fat-free milk at room temperature for 1 h and washed 3 times with TBST buffer solution for 10 min each time. Next, the primary antibody solution A11 (1 : 1000, OriGene, USA) and anti-catalase (1 : 1000, Abcam, UK) were added and incubated at 4°C overnight. The membrane was washed in the same way. Then, samples were incubated with IRDye®800CW goat-anti-rabbit antibody (1 : 5000, Abcam, UK) at room temperature for 1 h and visualized via chemiluminescence with an infrared laser scanning system (Odyssey LI-COR, USA).
10
Western Blotting of Antioxidant Proteins
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The preparation of tissue or cell extracts and a Western blot analysis were performed as previously described14 (link),21 (link). Rabbit polyclonal anti-UCP1 (Sigma), anti-PGC1α (Merk-Millipore), anti-catalase (Abcam) and anti-SOD1 antibody (ProteinTech) were used as the primary antibodies. Rat monoclonal anti-NRDC antibodies (#1, #135) were raised in our laboratory21 (link). Anti-α-tubulin (ProteinTech) and anti-β actin (Sigma) antibodies were used as the loading controls. To quantify the intensity of signals, a densitometric analysis was performed using ImageJ software.
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