Genegnome xrq chemidoc system

Manufactured by Syngene

Sourced in China, United States

The GeneGnome XRQ Chemidoc System is a high-performance imaging system designed for the detection and analysis of chemiluminescent and fluorescent signals in a variety of life science applications. The system features a sensitive charge-coupled device (CCD) camera, advanced optics, and a user-friendly software interface to capture and analyze images with precision.

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Lab products found in correlation

γh2ax, by Cell Signaling Technology (2 mentions) Gapdh, by Cell Signaling Technology (2 mentions) Bca protein assay reagent, by CWBIO (2 mentions) Odyssey machine, by LI COR (1 mentions) Hrp conjugated secondary antibody, by Vector Laboratories (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Dc protein assay kit, by Bio-Rad (1 mentions) Enhanced chemi luminescence (ecl), by Solarbio (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Phospho chk2 thr68, by Cell Signaling Technology (1 mentions) Phospho chk1 ser345, by Cell Signaling Technology (1 mentions) Recq1, by Santa Cruz Biotechnology (1 mentions) Rpa32, by Cell Signaling Technology (1 mentions) Enhanced chemiluminescence solution, by Advansta (1 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Beyotime (1 mentions)

4 protocols using genegnome xrq chemidoc system

Immunoblotting Quantification of Cellular Proteins

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Whole-cell lysates were prepared in radioimmunoprecipitation assay (RIPA) buffer containing protease inhibitor cocktail (Sigma, catalog no. 11873580001), and protein was quantified using Bio-Rad DC protein assay kit (Bio-Rad, catalog no. 5000111). Fifty microgram of total protein per lane was used for immunoblotting. The following primary antibodies were used: RECQL1 (1:1000; Bethyl Laboratories, catalog no. A300-450A), γH2AX (1:1000; Cell Signaling, catalog no. 2577), GAPDH (1:1000; Cell Signaling, catalog no. 5174), ERα (1:100, EP1 clone, Dako, catalog no. IS08430-2.), and β actin (1:10000; Abcam, catalog no. ab8226). Following incubation with infrared dye-labelled (Li-Cor) [IRDye 800CW Mouse Anti-Rabbit IgG and IRDye 680CW Rabbit Anti-Mouse IgG; 1:10000] or HRP-conjugated secondary antibodies (Vector Laboratories) for 1 h, membranes were scanned with a Li-Cor Odyssey machine (700 and 800nm) or GeneGnome XRQ Chemidoc System (Syngene) to determine protein expression and signal intensities were quantified using ImageJ.

Arora A., Parvathaneni S., Aleskandarany M.A., Agarwal D., Ali R., Abdel-Fatah T., Green A.R., Ball G.R., Rakha E.A., Ellis I.O., Sharma S, & Madhusudan S. (2016). Clinicopathological and functional significance of RECQL1 helicase in sporadic breast cancers. Molecular cancer therapeutics, 16(1), 239-250.

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Western Blot Analysis of GPNMB and Cyclin A

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Cell lysates were prepared in radioimmunoprecipitation (RIPA) buffer with protease inhibitor PMSF and Halt^TM phosphatase inhibitor cocktail (Roche, Switzerland). Protein concentrations were confirmed by BCA Protein Assay Reagent (CWBIO, China). Equivalent amounts of protein samples were separated by 12% SDS-PAGE, and the target proteins were transferred to PVDF membranes (Millipore, United States). Membranes were blocked in TBST, a blocking buffer containing 5% skim milk for 2 h at room temperature, followed by incubation with primary antibodies, including rabbit anti-GPNMB polyclonal antibody, rabbit anti-Cyclin A polyclonal antibody (1:1000, Santa Cruz Biotechnology, United States), and rabbit anti-β-actin polyclonal antibody (1:2000, CWBIO, China) at 4°C for overnight. After washes with TBST for five times, membranes were incubated with horseradish peroxidase HRP-conjugated goat anti-rabbit (or mouse) IgG (1:1000, CWBIO, China) for 2 h at room temperature. After washes with TBST for five times, immunoreactive bands were detected using chemiluminescent reagent ECL (Solarbio, China) by GeneGnome XRQ Chemidoc System (Syngene, Cambridge, United Kingdom). The cellular protein β-actin was measured as an internal control.

Guo K., Xu L., Wu M., Hou Y., Jiang Y., Lv J., Xu P., Fan Z., Zhang R., Xing F, & Zhang Y. (2019). A Host Factor GPNMB Restricts Porcine Circovirus Type 2 (PCV2) Replication and Interacts With PCV2 ORF5 Protein. Frontiers in Microbiology, 9, 3295.

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Immunoblotting Analysis of DNA Repair Proteins

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Forty-eight hours after siRNA transfection, cells were treated with HQ or BaP for 24 h as indicated. Where applicable, NU7026 (20 µM) and KU55933 (10 µM) were added 2 h before BaP treatment to inhibit DNA-PK and ATM, respectively; 0.1% DMSO was added to untreated cells. Subsequently, cells were washed with cold PBS and lysed in RIPA buffer (50 mM Tris-HCl [ph 8.0], 150 mM NaCl, 1% NP-40, 0.5% sodium deoxycholate, 0.1% SDS) containing protease and phosphatase inhibitors (Roche)). Equal amounts of total protein for each sample was used for immunoblotting with antibodies against RECQ1 (1:1000) and WRN (1:500) (Santa Cruz Biotechnology); RPA32, γH2AX, phospho-Chk1 Ser345, phospho-Chk2 Thr68, and GAPDH (all 1:1000, Cell Signaling). Images were captured using GeneGnome XRQ Chemidoc System (Syngene) and signal intensities were quantified using ImageJ.

Garige M, & Sharma S. (2014). Cellular deficiency of Werner Syndrome protein or RECQ1 promotes genotoxic potential of hydroquinone and benzo[a]pyrene exposure. International journal of toxicology, 33(5), 373-381.

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Western Blot Protocol for Protein Analysis

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Cells were collected with cold PBS at indicated time points, then treated with RIPA lysis buffer whichcontains 1 mM phenylmethyl sulfonylfluoride (PMSF) (Beyotime, Beijing, China) on ice for 30 min. Protein concentration was confirmed using BCA Protein Assay Reagent (CWBIO, Beijing, China). Equivalent amounts of protein samples were separated by 12% SDS–PAGE and target protein were transferred to PVDF membranes. Membranes were blocked with 5% skim milk and then incubated with primary antibodies over night at 4 °C, followed by HRP-conjugated secondary antibodies. Signals were visualized by enhanced chemiluminescence solution (Advansta, USA) and using GeneGnome XRQ Chemidoc System (Syngene, Cambridge, UK) to obtain images.

Ning P., Zhou Y., Liang W, & Zhang Y. (2016). Different RNA splicing mechanisms contribute to diverse infective outcome of classical swine fever viruses of differing virulence: insights from the deep sequencing data in swine umbilical vein endothelial cells. PeerJ, 4, e2113.

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