Chemidoc xrs chemiluminescence detection and imaging system

Manufactured by Bio-Rad

The ChemiDoc XRS is a chemiluminescence detection and imaging system designed for life science research. It captures and analyzes images of chemiluminescent samples, such as Western blots, for quantitative analysis of protein expression and other applications.

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Lab products found in correlation

Polyvinylidene difluoride membrane, by Merck Group (5 mentions) Ripa buffer, by Santa Cruz Biotechnology (3 mentions) Hrp conjugated secondary antibody, by Jackson ImmunoResearch (3 mentions) Ab134185, by Abcam (2 mentions) Anti ha 51064 2 ap, by Proteintech (2 mentions) Anti e cadherin, by BD (2 mentions) Anti tubulin, by Abcam (2 mentions) P stat3, by Cell Signaling Technology (2 mentions) Bis tris gel, by Thermo Fisher Scientific (2 mentions) Stat3 9132, by Cell Signaling Technology (2 mentions) Anti dkk1 21112 1 ap, by Proteintech (1 mentions) Anti flag 20543 1 ap, by Proteintech (1 mentions) Anti gapdh 10494 1 ap, by Proteintech (1 mentions) Quantity one software, by Bio-Rad (1 mentions) Pathscan stress and apoptosis signaling antibody array kit, by Cell Signaling Technology (1 mentions) Ab8227, by Abcam (1 mentions) Anti β actin, by Merck Group (1 mentions) Anti 4 hne, by Abcam (1 mentions) Anti flag, by Proteintech (1 mentions) Anti vinculin, by Proteintech (1 mentions)

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10 protocols using chemidoc xrs chemiluminescence detection and imaging system

Western Blot Analysis of Protein Targets

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In western blotting, cells were lysed in 1× SDS loading buffer (50 mM Tris-HCl pH6.8, 10% glycerol, 2% SDS, 0.05% bromophenol blue, and 1% 2-mercaptoethanol). Antibodies were listed as follows: anti-ZBTB38 antibody (21906-1-AP, Proteintech), anti-DKK1 (21112-1-AP, Proteintech), anti-PRKDC (SC-5282, Santa Cruz), anti-HA (51064-2-AP, Proteintech), anti-FLAG (20543-1-AP, Proteintech), anti-GAPDH (10494-1-AP, Proteintech), and anti-TUBULIN (ab134185, Abcam).
We did immunoblot as previously described [22 (link)]. In brief, all proteins were separated by SDS–PAGE and were transferred to polyvinylidene difluoride membranes (Millipore). Horseradish peroxidase-labeled secondary antibodies and an enhanced chemiluminescence system were used for signal detection. Protein was visualized using ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories) or KODAK film machine.

Ding G., Lu W., Zhang Q., Li K., Zhou H., Wang F., Zhao C., Fan C, & Wang J. (2021). ZBTB38 suppresses prostate cancer cell proliferation and migration via directly promoting DKK1 expression. Cell Death & Disease, 12(11), 998.

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Multiplex Signaling Profiling in Tumors

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Eight tumor samples were randomly selected from each group for all the following molecular analyses in tumors. A slide-based antibody array was used for simultaneous detection of 19 important signaling molecules involved in stress response and apoptosis, using a PathScan Stress and Apoptosis Signaling Antibody Array kit (Cell Signaling Technology, Danvers, MA) following the manufacturer’s instructions. Each of these molecules was detected in duplicate on the same array arranged as shown in Fig. 2c, and the identity of each numbered molecule listed in Fig. 2d. Briefly, total protein was extracted from tumor tissues using RIPA buffer (Santa Cruz Technology, CA), and diluted to 0.5 mg/mL in Array Diluent Buffer provided by the kit. The protein samples were incubated with the array antibodies overnight. A Detection Antibody Cocktail was added to the samples, followed by the addition of HRP-linked Streptavidin and substrate. Protein was visualized using a ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories, Irvine, CA). The density of the spots were quantitated using Quantity One software (Bio-Rad Laboratories) and normalized to the α-tubulin levels. Each sample was done in duplicate.

Wang P., Henning S.M., Magyar C.E., Elshimali Y., Heber D, & Vadgama J.V. (2016). Green tea and quercetin sensitize PC-3 xenograft prostate tumors to docetaxel chemotherapy. Journal of Experimental & Clinical Cancer Research : CR, 35, 73.

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Western Blotting Protocol for Protein Analysis

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In western blotting, cells were lysed in 1 × SDS loading buffer (50 mM Tris–HCl pH6.8, 10% glycerol, 2% SDS, 0.05% bromophenol blue and 1% 2-mercaptoethanol). Antibodies were listed as follows: anti-PGM5 antibody (NBP2-62654, Novus Biologicals) and anti-ACTIN (ab8227, Abcam).
We did immunoblot as previously described [18 (link)]. In brief, all proteins were separated by SDS–PAGE and were transferred to polyvinylidene difluoride membranes (Millipore). HRP-labeled secondary antibodies and enhanced chemiluminescence system was used for signal detection. Protein was visualized using ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories) or KODAK film machine.

Sun J., Wang F., Zhou H., Zhao C., Li K., Fan C, & Wang J. (2022). Downregulation of PGM5 expression correlates with tumor progression and poor prognosis in human prostate cancer. Discover. Oncology, 13, 63.

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Western Blot Protein Analysis

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Cells were lysed using 1× SDS loading buffer (50 mM Tris-HCl pH 6.8, 10% glycerol, 2% SDS, 0.05% bromophenol blue, and 1% 2-mercaptoethanol). Antibodies were purchased from the manufacturers as follows: anti-LanCL1 antibody (Proteintech), anti-4-HNE (Abcam), anti-E-cadherin (610181, BD Transduction Laboratories), anti-pSAPK/JNK (Thr183/Try185) (Cell Signaling Technology), anti-β-actin (Sigma–Aldrich), and anti-tubulin (Abcam). For immunoblot, proteins were separated by SDS–PAGE and transferred to polyvinylidene difluoride membranes (Millipore). HRP-conjugated secondary antibodies (Jackson Laboratories) and enhanced chemiluminescence system was used for signal detection. Protein was visualized using KODAK film machine or ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories).

Wang J., Xiao Q., Chen X., Tong S., Sun J., Lv R., Wang S., Gou Y., Tan L., Xu J., Fan C, & Ding G. (2018). LanCL1 protects prostate cancer cells from oxidative stress via suppression of JNK pathway. Cell Death & Disease, 9(2), 197.

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SDS-PAGE and Immunoblotting Protocol

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Cells were lysed using 1× SDS loading buffer (50 mM Tris‐HCl pH6.8, 10% glycerol, 2% SDS, 0.05% bromophenol blue and 1%2‐mercaptoethanol).Antibodies were listed as follows: anti‐HNF1B antibody (Proteintech), anti‐Cyclin D1 (610 181, BD Transduction Laboratories), anti‐SMAD6, anti‐p‐SMAD2/3, anti‐FLAG (Proteintech), anti‐Vinculin (Proteintech) and anti‐tubulin (Abcam). For immunoblot, proteins were separated by SDS–PAGE and transferred to polyvinylidene difluoride membranes (Millipore). HRP‐conjugated secondary antibodies (Jackson laboratories) and enhanced chemiluminescence system were used for signal detection. Protein was visualized using KODAK film machine or ChemiDoc XRS chemiluminescence detection and imaging system (Bio‐Rad Laboratories).

Lu W., Sun J., Zhou H., Wang F., Zhao C., Li K., Fan C., Ding G, & Wang J. (2020). HNF1B inhibits cell proliferation via repression of SMAD6 expression in prostate cancer. Journal of Cellular and Molecular Medicine, 24(24), 14539-14548.

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Phospho-Protein Profiling in Prostate Cancer Cells

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A slide-based antibody array was used for simultaneous detection of 18 important and well-characterized signaling molecules when phosphorylated or cleaved using a PathScan Intracellular Signaling Array kit (Cell Signaling Technology, Danvers, MA) following the manufacturer's instructions. The list of these molecules is shown in Fig. 3C. When 50-60% confluent in T25 Petri dishes, both LAPC-4 and LNCaP cells were treated with vehicle control (DMSO), 1μM Arc, 10μM Q, or 1μM Arc + 10μM Q for 48h. Total protein was extracted using RIPA buffer (Santa Cruz Technology, CA), and diluted to 0.5 mg/mL in Array Diluent Buffer provided by the kit. After an overnight incubation of the samples with the array antibodies, a Detection Antibody Cocktail was added to the samples, followed by the addition of HRP-linked Streptavidin and substrate. Protein was visualized using a ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories, Irvine, CA).

Wang P., Phan T., Gordon D., Chung S., Henning S.M, & Vadgama J.V. (2014). Arctigenin in combination with quercetin synergistically enhances the anti-proliferative effect in prostate cancer cells. Molecular nutrition & food research, 59(2), 250-261.

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Western Blot Analysis of EMT Markers

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Cells were lysed using 1× SDS loading buffer (50 mM Tris-HCl pH 6.8, 10% glycerol, 2% SDS, 0.05% bromophenol blue, and 1% 2-mercaptoethanol). Antibodies were listed as follows: anti-HNF1B antibody (12533-1-AP, Proteintech), anti-E-cadherin (610181, BD Transduction Laboratories), anti-SLUG (C19G7, Cell Signaling Technology), anti-SNAI1 (C15D3, Cell Signaling Technology), anti-EZH2 (AC22, Cell Signaling Technology), anti-HA (51064-2-AP, Proteintech), anti-FLAG (20543-1-AP, Proteintech), anti-RBBP7 (20365-1-AP, Proteintech), and anti-tubulin (ab134185, Abcam). For immunoblot, proteins were separated by SDS–PAGE and transferred to polyvinylidene difluoride membranes (Millipore). HRP-conjugated secondary antibodies (Jackson laboratories) and enhanced chemiluminescence system was used for signal detection. Protein was visualized using KODAK film machine or ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories).

Wang J., He C., Gao P., Wang S., Lv R., Zhou H., Zhou Q., Zhang K., Sun J., Fan C., Ding G, & Lan F. (2019). HNF1B-mediated repression of SLUG is suppressed by EZH2 in aggressive prostate cancer. Oncogene, 39(6), 1335-1346.

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Investigating Molecular Mechanisms of Phytochemicals

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When 50–60% confluent in 60 mm Petri dishes, both LNCaP and MCF-7 cells were treated with vehicle control, 40μM EGCG, 1μM arctigenin, 2mg/L curcumin, 2mg/L curcumin + 40μM EGCG, 2mg/L curcumin + 1μM arctigenin, or 2mg/L curcumin + 40μM EGCG + 1μM arctigenin for 48h. The procedure for cell harvest and protein extraction was described before ²³. For the Western blot analysis, 50 μg of protein was loaded and separated on a 4–12% Bis-Tris gel (Invitrogen, Carlsbad, CA). Proteins were electrotransferred to nitrocellulose membranes and blocked in Tris-buffered saline with 0.1% Tween 20 and 5% nonfat milk for 1 hour at room temperature. Membranes were incubated with primary anti-human antibodies for the detection of Bax (sc-493), Bcl-2 (sc-509, Santa Cruz Technology, CA), NFκB (3034), p-NFκB (3031), p-NFκB inhibitor protein (IκB)-α (2859), Akt (4685), p-Akt (Ser473) (4058), Stat3 (9132), and p-Stat3 (9131, Cell Signaling Technology, Danvers, MA). GAPDH protein was used as loading control. Protein was visualized and analyzed using a ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories, Irvine, CA). The experiment was done in duplicate and repeated twice.

Wang P., Wang B., Chung S., Wu Y., Henning S.M, & Vadgama J.V. (2014). Increased chemopreventive effect by combining arctigenin, green tea polyphenol and curcumin in prostate and breast cancer cells. RSC advances, 4(66), 35242-35250.

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Western Blot Analysis of ITGB4 Expression

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Cells were lysed using RIPA protein extraction buffer (cat. no. P0013B) with PSMF (cat. no. ST505; Beyotime Institute of Biotechnology) and 1X SDS loading buffer. Protein concentration was determined using bicinchoninic acid (BCA) method. A total of 20 µg protein was loaded per lane. The proteins were transferred to polyvinylidene difluoride (PVDF) membrane. Blocking was conducted using QuickBlock™ blocking buffer (cat. no. P0252; Beyotime Institute of Biotechnology) for 15 min at room temperature. TBST with 1% Tween 20 was used for washing. The membrane was incubated at 4°C overnight with the following primary antibodies: anti-ITGB4 antibody (1:1,000; cat. no. 14803) and anti-GAPDH (1:1,000; cat. no. 2118; both from Cell Signaling Technology, Inc.). Subsequently, membranes were incubated at room temperature for 2 h with HRP-conjugated anti-rabbit IgG secondary antibody (1:5,000; cat. no. 7074; Cell Signaling Technology, Inc.). Protein bands were visualized using a ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories, Inc.).

Lu X., Ma S., Li Y., Pan Y, & Kang N. (2023). Identification of ITGB4 as a novel tumor promoting gene in lung adenocarcinoma (LUAD). Oncology Reports, 51(2), 30.

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Evaluation of EGCG, Quercetin, and Docetaxel Effects on Prostate Cancer Cells

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LAPC-4-AI and PC-3 cells were treated with vehicle control, 40μM EGCG+5μM Q, 5nM Doc, or EGCG+Q+Doc for 48h. Total protein was extracted using RIPA buffer (Santa Cruz Technology, CA). The procedure for Western blot analysis was described before [31 ]. Briefly, 50 μg of protein was separated on a 4–12% Bis-Tris gel (Invitrogen, Carlsbad, CA). Proteins were electrotransferred to nitrocellulose membranes. Membranes were incubated with primary anti-human antibodies for the detection of Bax (sc-493), Bcl-2 (sc-509), MRP1 (sc-7773, Santa Cruz Technology), Akt (4685), p-Akt (Ser473, 4058), STAT3 (9132), and p-STAT3 (4058, Cell Signaling Technology, Danvers, MA). GAPDH protein was used as loading control. Protein was visualized and analyzed using a ChemiDoc XRS chemiluminescence detection and imaging system (Bio-Rad Laboratories, Irvine, CA).

Wang P., Henning S.M., Heber D, & Vadgama J.V. (2015). Sensitization to docetaxel in prostate cancer cells by green tea and quercetin. The Journal of nutritional biochemistry, 26(4), 408-415.

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