After bladder tissues were homogenized in RIPA buffer, whole cell homogenates were centrifuged at 13,000 ×g, 4°C for 20 min and the supernatants were collected. Each supernatant was loaded onto acrylamide gels and separated by SDS-PAGE. The proteins in the gel were then transferred onto a nitrocellulose membrane, after which the membranes were stained with Ponceau to check for uniform protein loading. After blocking the membranes, they were incubated overnight at 4°C with the following antibodies: JNK (#3708), Phospho-JNK (#9251), p38 (#9212), Phospho-p38 (#9211, Cell Signaling Technology, MA, USA), xanthine oxidase (SC-22006), ERK1 (SC-94), Phospho-ERK1 (SC-7383), Bax (SC-493), Bcl-2 (SC-7382), and GAPDH (SC-25778, Santa Cruz Biotechnology, CA, USA).
Xanthine oxidase
Manufactured by Santa Cruz Biotechnology
Sourced in United States
Xanthine oxidase is an enzyme that catalyzes the oxidation of xanthine to uric acid. It is a molybdenum-containing enzyme that plays a role in purine metabolism.
Automatically generated - may contain errors
Lab products found in correlation
Phospho jnk, by Cell Signaling Technology (1 mentions)
Phospho p38, by Cell Signaling Technology (1 mentions)
Gapdh, by Santa Cruz Biotechnology (1 mentions)
Bcl2 associated x (bax), by Santa Cruz Biotechnology (1 mentions)
Bcl 2, by Santa Cruz Biotechnology (1 mentions)
Stem cell factor (scf), by Santa Cruz Biotechnology (1 mentions)
P creb, by Cell Signaling Technology (1 mentions)
Enhanced chemiluminescence solution, by Thermo Fisher Scientific (1 mentions)
Basic fibroblast growth factor (bfgf), by Cell Signaling Technology (1 mentions)
Anti mouse or anti rabbit horseradish peroxidase conjugated antibodies, by Thermo Fisher Scientific (1 mentions)
Stem cell factor (scf), by Abcam (1 mentions)
Basic fibroblast growth factor (bfgf), by R&D Systems (1 mentions)
β actin, by Merck Group (1 mentions)
Las 3000, by Fujifilm (1 mentions)
2 protocols using xanthine oxidase
1
Immunoblotting analysis of bladder proteins
2
Protein Expression Analysis in Cell Cultures
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Equal amounts of extracted proteins were resolved and transferred to nitrocellulose membranes. These membranes were incubated with antibodies to GDA, tyrosinase, SCF, xanthine oxidase (mouse monoclonal; Santa Cruz Biotechnology, Dallas, TX, USA), MITF, bFGF, p-CREB, CREB (rabbit polyclonal; cell signaling technology, Beverly, MA, USA), and β-actin (mouse monoclonal; Sigma-Aldrich). After incubating with appropriate anti-mouse or anti-rabbit horseradish peroxidase-conjugated antibodies (Thermo Fisher Scientific, Waltham, MA, USA) or with anti-goat horseradish peroxidase-conjugated antibody (Santa Cruz Biotechnology), enhanced chemiluminescence solution (Thermo Fisher Scientific) was applied and signals were captured with an image reader (LAS-3000; Fuji Photo Film, Tokyo, Japan). Protein bands were then analyzed by densitometry. Concentrations of bFGF (R&D Systems, Minneapolis, MN, USA) and SCF (Abcam) in culture supernatants were measured using ELISA kits according to the manufacturer’s instructions.
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