G box ichemi xr

Manufactured by Syngene

Sourced in United Kingdom, United States

The G:BOX iChemi XR is a high-performance imaging system designed for DNA and protein gel documentation. It features a sensitive CCD camera, adjustable UV transilluminator, and advanced software for capturing and analyzing gel images. The system is capable of detecting a wide range of fluorescent and chemiluminescent signals.

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Lab products found in correlation

Par1c mark1, by Proteintech (2 mentions) Genesnap software version 7.09 a, by Syngene (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Phosphatase inhibitor cocktail, by Merck Group (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Thermo Fisher Scientific (1 mentions) Ecl plus, by Beyotime (1 mentions) Nitrocellulose membrane, by GE Healthcare (1 mentions) Chemiluminescence detection reagent, by Bio-Rad (1 mentions) Enhanced chemiluminescence detection reagent, by Bio-Rad (1 mentions) Qiashredder, by Qiagen (1 mentions) P53 sc 6243, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

G:BOX (415 citations) G:BOX iChemi (4 citations)

8 protocols using g box ichemi xr

Western Blot Analysis of Par1/MARK Proteins

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Primary microglia cultures were lysed with RIPA buffer (20 mM Tris-HCl, 150 mM NaCl, 0.5% NP40, 1.0% Trition-X 100, 2.0 mM EDTA, 2.0 mM EGTA, and 0.25% DOC) and supplemented with protease inhibitor cocktail (Sigma Aldrich, Saint Louis, MO), phosphatase inhibitor cocktail (Sigma Aldrich, Saint Louis, MO), 10 mM β-glycerophosphate, 10 mM NaF, 10 mM Dithiothreitol (DTT), and 10 mM Phenylmethylsulfonyl fluoride (PMSF). Lysed cells were incubated on ice for 10 min and centrifuged at 13,000×g at 4 °C for 10 min. Thirty micrograms cleared lysate was run on a 10% SDS-PAGE gel and transferred to PVDF membrane. Blots were probed with primary antibodies for three out of the four Par1/MARK family members: Par1a/MARK3 (Millipore, Germany: 1:1000; UpState Cell Signaling Solutions, Lake Placid, NY: 1:1000), Par1b/MARK2 (ProteinTech, Rosemont, IL: 1:1000), and Par1c/MARK1 (ProteinTech, Rosemont, IL: 1:1000). Horseradish peroxidase conjugated goat anti-rabbit, and goat anti-mouse antibodies (Jackson ImmunoResearch, West Grove, PA) were used at 1:5000. Imaging of blots by enhanced chemiluminescence was performed using Syngene G:Box/iChemi-XR and the GeneSnap software (Version 7.09.a) (Syngene, Frederick, MD).

DiBona V.L., Zhu W., Shah M.K., Rafalia A., Ben Cheikh H., Crockett D.P, & Zhang H. (2019). Loss of Par1b/MARK2 primes microglia during brain development and enhances their sensitivity to injury. Journal of Neuroinflammation, 16, 11.

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Analysis of Par1 Signaling in Primary Neurons

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Primary cortical neuron cultures were lysed in RIPA buffer (20mM Tris-HCl, 150mM NaCl, 0.5% NP40, 1.0% Trition-X, 2.0mM EDTA, 2.0mM EGTA, and 0.25% DOC) supplemented with protease inhibitor cocktail (Sigma Aldrich, Saint Louis, MO), phosphatase inhibitor cocktail (Sigma Aldrich, Saint Louis, MO), 10 mM β-glycerophosphate, 10 mM NaF, 10 mM Dithiothreitol (DTT), and 10 mM Phenylmethylsulfonyl fluoride (PMSF). Lysed cells were incubated on ice for 10 minutes and centrifuged at 13,000xg at 4°C for 10 min to obtain cleared lysate. 30μg of total lysate was run on 10% SDS-PAGE gels and transferred to PVDF membrane. Blots were probed with primary antibodies Par1c/MARK1 (ProteinTech, Rosemont, IL: 1:1000) and p-Par1 (Cell Signaling, Danvers, MA: 1:1000). Horseradish peroxidase conjugated goat anti-rabbit and goat anti-mouse antibody (Jackson ImmunoResearch, West Grove, PA) was used at 1:5,000. Imaging of blots by enhanced chemiluminescence was obtained using Syngene G:Box/iChemi-XR and the GeneSnap software (Version 7.09.a) (Syngene, Frederick, MD).

DiBona V.L., Shah M.K., Krause K.J., Zhu W., Voglewede M.M., Smith D.M., Crockett D.P, & Zhang H. (2021). Metformin reduces neuroinflammation and improves cognitive functions after traumatic brain injury. Neuroscience research, 172, 99-109.

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Western Blot Protein Detection

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Cells were lysed with lysing buffer, supplemented with protease inhibitor cocktail, and then protein concentrations were measured by BCA assay. Equal amounts of total protein from different samples were subjected to 10% SDS-polyacrylamide gels and then transferred to polyvinylidenedifluoride membranes, which were probed with the indicated primary antibodies. Detection was accomplished using corresponding horseradish peroxidase (HRP)-conjugated secondary antibodies followed by development with ECL Plus (Beyotime Co., Suzhou, Jiangsu Province, China). Images were captured by G: BOX iChemi XR (Syngene Inc., UK). The intensities of the bands were analyzed by Image J2x software. Cell lysing solution, protease inhibitor cocktail, BCA protein assay kit, and chemiluminescent substrate were purchased from Thermo Scientific (Pierce, Rockford, MA, USA).

Xu L.M., Zheng Y.J., Wang Y., Yang Y., Cao F.F., Peng B., Xu X.F., An H.Z., Zheng A.X., Zhang D.H., Uzan G, & Yu Y.Z. (2014). Celastrol Inhibits Lung Infiltration in Differential Syndrome Animal Models by Reducing TNF-α and ICAM-1 Levels while Preserving Differentiation in ATRA-Induced Acute Promyelocytic Leukemia Cells. PLoS ONE, 9(8), e105131.

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Cell Lysis Protein Extraction and Western Blot

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Cells were incubated in lysis buffer and cleared by centrifugation at 13,000 × g for 10 min. For the phosphorylation protein assay, phosphatase inhibitor was added to suppress the activity of phosphatase. The extraction of cytoplasmic and nuclear protein was performed according to product manufacturer instructions. A BCA protein assay reagent kit determined protein concentrations. Aliquots of samples were subjected to 10% SDS-polyacrylamide gels and then transferred to polyvinylidenedifluoride (PVDF) membranes. Membranes were probed with the indicated antibodies. Detection was accomplished using corresponding horseradish peroxidase (HRP)-conjugated secondary antibodies followed by development with Beyo ECL Plus; pictures were captured by G: BOX iChemi XR (Syngene Inc., UK).

Peng B., Zhang X., Cao F., Wang Y., Xu L., Cao L., Yang C., Li M., Uzan G, & Zhang D. (2014). Peptide deformylase inhibitor actinonin reduces celastrol’s HSP70 induction while synergizing proliferation inhibition in tumor cells. BMC Cancer, 14, 146.

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Histone Extraction and Phospho-H2AX Analysis

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After HL-60 cells were treated, histones were extracted from 3 × 10⁶ cells, subjected to 15% PAGE, and analyzed by western blots as described previously [31 (link)]. Chemiluminescent images were captured using G:Box iChemi XR (Syngene). Mouse monoclonal anti-phospho-histone H2AX antibody (clone JBW301) was from EMD Millipore.

Ishiguro K., Lin Z.P., Penketh P.G., Shyam K., Zhu R., Baumann R.P., Zhu Y.L., Sartorelli A.C., Rutherford T.J, & Ratner E.S. (2014). Distinct mechanisms of cell-kill by triapine and its terminally dimethylated derivative Dp44mT due to a loss or gain of activity of their copper(II) complexes. Biochemical pharmacology, 91(3), 312-322.

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Cerebral Cortex Protein Extraction and Western Blot

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The cerebral cortex tissue of the rat was homogenized in 20 mM Tris, 100 mM NaCl, 1 mM EDTA, 1 mM DTT pH 7.5, buffer consisting of protease inhibitor cocktail, and the homogenate was centrifuged at 12,000 g for 25 minutes to collect the supernatant. The protein concentration was measured by the Lowry method. An equal amount of the cerebral cortex protein, 30 to 80 μg was used to perform SDS-polyacrylamide gel electrophoresis using 12% gel. After SDS-polyacrylamide gel electrophoresis, the proteins were transferred onto a nitrocellulose membrane (GE Healthcare). Nonspecific binding was blocked by using 5% skimmed milk powder (Himedia Laboratories, India) in phosphate buffer saline with 0.1% Tween 20 (PBST, pH 7.5) for 120 minutes and incubated overnight at 4 °C with primary antibodies, then washed with PBST (3 times, 10 minutes each) followed by horseradish peroxidase conjugated secondary antibodies for 90 minutes and washed with PBST (3 times, 10 minutes each). The immunoblots were treated with chemiluminescence detection reagents (Bio-Rad, California, USA) and captured images in an Image Analyzer (G-Box iChemi XR, Syngene, Maryland, USA) then analyzed and quantitated using ImageJ software (National Institutes of Health).

Savitikadi P., Palika R., Pullakhandam R., Reddy G., & Reddy S. (2023). Dietary zinc inadequacy affects neurotrophic factors and proteostasis in the rat brain. Nutrition Research, 116, 80-88.

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Western Blot Analysis of Lung Proteins

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Lung tissue was homogenised in 20 mM Tris lysis buffer (100 mM NaCl, 1 mM EDTA, 1 mM DTT, 1 mM PMSF, 1 µg/mL each of aprotinin, leupeptin, and pepstatin; pH7.5) and protein concentration was measured by the Lowry method. An equal amount of protein from each of the three experimental groups was subjected to SDS PAGE and the resolved bands were transferred to nitrocellulose membrane to probe with primary antibodies each at a specific dilution. Then incubated with respective secondary antibody conjugated with HRP enzyme. Finally, the bands are visualised after developing with enhanced chemiluminescence detection reagent (Bio-Rad Laboratories, California, USA) and images were captured by an Image Analyzer (G-Box iChemi XR; Syngene, Maryland, USA). Images were quantitated and analyzed using ImageJ software (NIH, Bethesda, USA).

Nagaraju M., Kalahasti K.K., Reddy K.P., Addi U.R., Satyavani M., Reddy G.B, & Reddy S.S. (2022). Anti-inflammatory potential of turmeric, amla, and black pepper mixture against sepsis-induced acute lung injury in rats. Journal of Food Science and Technology, 60(1), 252-261.

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Protein Expression Analysis of DNA Repair Factors

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EOC cells seeded at 1.5 × 10⁶ cells/75 cm²-flask were allowed to adhere overnight and treated with carboplatin or triapine for 24 h. Trypsinized cells were washed once with phosphate buffered saline (PBS) and solubilized in 200 µl of Laemmli’s sample buffer at 100°C for 5 min. The lysates were further passed through a QIAshredder (QIAGEN, Valencia, CA) to shear DNA. The extracts were resolved by 6% or 15% polyacrylamide gel electrophoresis (PAGE). Chemiluminescent images were captured using G:Box iChemi XR (Syngene, Frederick, MD). Antibodies to the following proteins were purchased: p53 (sc-6243, Santa Cruz Biotechnology, Santa Cruz, CA); BRCA2 (MAB2476, R&D Systems, Minneapolis, MN); Rad51 (MS-988, clone 3C10, Thermo Scientific, Fremont, CA); RPA70 (MS-692, Thermo Scientific), PCNA (MS-106, clone PC10, Thermo Scientific); γH2AX (sc-101696, Santa Cruz); deoxycytidine kinase (MABC188, clone 9D4, EMD Millipore, Temecula, CA); O⁶-methylguanine-DNA methyltransferase (MAB16200, clone MT 3.1, EMD Millipore).

Ishiguro K., Zhu Y.L., Lin Z.P., Penketh P.G., Shyam K., Zhu R., Baumann R.P., Sartorelli A.C., Rutherford T.J, & Ratner E.S. (2016). Cataloging antineoplastic agents according to their effectiveness against platinum-resistant and platinum-sensitive ovarian carcinoma cell lines. Journal of translational science, 2(2), 117-124.

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