G box chemi xrq chemiluminescence imager

Manufactured by Syngene

Sourced in United Kingdom

The G:BOX Chemi XRQ is a chemiluminescence imager designed for detecting and quantifying chemiluminescent signals from a variety of sample types. It features a high-resolution CCD camera and a light-tight darkroom enclosure to capture images with high sensitivity and low background noise.

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5 protocols using g box chemi xrq chemiluminescence imager

Western Blot Analysis of Signaling Proteins

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Proteins were resolved by standard 10% SDS–PAGE and electroblotted onto nitrocellulose membranes. Membranes were blocked with 4% bovine serum albumin (w/v) in TBST, and protein bands were detected with specific antibodies using chemiluminescence reagents and a G:BOX Chemi XRQ chemiluminescence imager (Syngene).
The following rabbit antibodies were used: anti‐IκBα (1:1,000; Cell Signaling), anti‐phospho‐p38 (1:1,000; Cell Signaling), anti‐phospho‐SAPK/JNK (1:1,000; Cell Signaling) and anti‐phospho‐ERK (1:1,000; Santa Cruz Biotechnology). Immunoreactive bands were visualised by incubation with horseradish peroxidase‐conjugated goat anti‐rabbit immunoglobulins (1:5,000) or goat anti‐mouse immunoglobulins (1:1,000; Bio‐Rad). To ensure that equal amounts of proteins were loaded, blots were re‐probed with α‐tubulin (1:3,000; Sigma‐Aldrich).
To detect multiple proteins, membranes were re‐probed after stripping of previously used antibodies using a pH 2.2 glycine‐HCl/SDS buffer.

Kidd T.J., Mills G., Sá‐Pessoa J., Dumigan A., Frank C.G., Insua J.L., Ingram R., Hobley L, & Bengoechea J.A. (2017). A Klebsiella pneumoniae antibiotic resistance mechanism that subdues host defences and promotes virulence. EMBO Molecular Medicine, 9(4), 430-447.

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Western Blot Analysis of Protein Interactions

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Proteins resolved by 15% SDS-PAGE and electroblotted onto nitrocellulose membranes. Membranes were blocked with 4% bovine serum albumin (w/v) in PBS and protein bands were detected with specific antibodies using chemiluminescence reagents and a G:BOX Chemi XRQ chemiluminescence imager (Syngene). The following antibodies were used: anti-Flag antibody (1:2,000; Sigma), anti-VSVG antibody (1:2,000; Sigma). Immunoreactive bands were visualized by incubation with horseradish peroxidase-conjugated goat anti-rabbit immunoglobulins (1:5000, BioRad 170–6515) or goat anti-mouse immunoglobulins (1:5000, BioRad 170–6516). To ensure that equal amounts of proteins were loaded, membranes were reprobed after stripping of previously used antibodies using a pH 2.2 glycine-HCl/SDS buffer with anti-E.coli RNA Polymerase α (1:2,000; BioLegend 663102).
GST fusions in yeast were immunodetected with primary rabbit polyclonal anti-GST (Z-5) antibody (1:2000, Santa Cruz Biotechnology). Secondary antibodies were IRDye-680 or IRDye -800 anti-rabbit and detection was performed with an Odyssey Infrared Imaging System (LI-COR Biosciences).

Storey D., McNally A., Åstrand M., sa-Pessoa Graca Santos J., Rodriguez-Escudero I., Elmore B., Palacios L., Marshall H., Hobley L., Molina M., Cid V.J., Salminen T.A, & Bengoechea J.A. (2020). Klebsiella pneumoniae type VI secretion system-mediated microbial competition is PhoPQ controlled and reactive oxygen species dependent. PLoS Pathogens, 16(3), e1007969.

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Western Blot Analysis of Immune Signaling

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Lysates were prepared in lysis buffer (1x SDS Sample Buffer, 62.5 mM Tris-HCl pH 6.8, 2% w/v SDS, 10% glycerol, 50 mM DTT, 0.01% w/v bromophenol blue). Proteins were resolved by standard 10% SDS-PAGE and electroblotted onto nitrocellulose membranes. Membranes were blocked with 4% bovine serum albumin (w/v) in TBST and protein bands were detected with specific antibodies using chemiluminescence reagents and a G:BOX Chemi XRQ chemiluminescence imager (Syngene). The following rabbit antibodies were used: anti-phospho IRF3 (Ser 396) (1:1000; Cell Signaling #4947), anti-phospho-TBK1 (Ser 172) (1:1000; Cell Signaling #5483), and anti-ISG15 (1:1000; Cell Signaling #9636). Immunoreactive bands were visualized by incubation with horseradish peroxidase-conjugated goat anti-rabbit immunoglobulins (1:5000) or goat anti-mouse immunoglobulins (1:1000; Bio-Rad). To ensure that equal amounts of proteins were loaded, blots were re-probed with α-tubulin (1:3000; Sigma-Aldrich). To detect multiple proteins, membranes were re-probed after stripping of previously used antibodies using a pH 2.2 glycine-HCl/SDS buffer.

Ivin M., Dumigan A., de Vasconcelos F.N., Ebner F., Borroni M., Kavirayani A., Przybyszewska K.N., Ingram R.J., Lienenklaus S., Kalinke U., Stoiber D., Bengoechea J.A, & Kovarik P. (2017). Natural killer cell-intrinsic type I IFN signaling controls Klebsiella pneumoniae growth during lung infection. PLoS Pathogens, 13(11), e1006696.

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Western Blot Analysis of Signaling Proteins

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Proteins were resolved on standard 10% SDS-PAGE gels and electroblotted in a semidry manner onto nitrocellulose membranes. Membranes were subsequently blocked with 3% (wt/vol) bovine serum albumin in TBS-Tween (TBST), and specific antibodies were used to detect protein using chemiluminescence reagents and a G:BOX Chemi XRQ chemiluminescence imager (Syngene).
All antibodies were probed with a secondary goat anti-rabbit/mouse antibody conjugated to IgG horseradish peroxidase, diluted 1:5,000 (no. 170-6515/170-6516; Bio-Rad). Antibodies used in this study were anti-IκBα (anti-rabbit, 1:1,000; no. 4812S; Cell Signaling), anti-phospho-JNK (anti-rabbit, 1:1,000; no. 9251S; Cell Signaling), anti-phospho-ERK (anti-rabbit, 1:1,000; no. 9101; Cell Signaling), anti-phospho-CREB (anti-rabbit, 1:1,000; no. sc-7978-R; Santa Cruz Biotechnology), and anti-phospho-p38 (anti-rabbit, 1:1,000; no. 4511; Cell Signaling). To ensure that equal amounts of proteins were loaded, blots were reprobed with α-tubulin (anti-mouse, 1:4,000; no. T5168; Sigma-Aldrich).
To detect multiple proteins, membranes were reprobed after stripping of previously used antibodies using a pH 2.2 glycine‐HCl–SDS buffer.
Bands were analyzed using ImageJ with the Histogram analysis tool, and results were expressed as a percentage of the intensity of the band found in the samples from cells infected with the wild-type strain.

Bartholomew T.L., Kidd T.J., Sá Pessoa J., Conde Álvarez R, & Bengoechea J.A. (2019). 2-Hydroxylation of Acinetobacter baumannii Lipid A Contributes to Virulence. Infection and Immunity, 87(4), e00066-19.

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Immunoblotting Protocol for Protein Analysis

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Samples were homogenized in RIPA buffer containing protease inhibitor cocktail (Sigma) and PhosSTOP™ (Roche). Protein concentrations were normalized by using Pierce BCA protein assay kit (Thermo Fisher, Catalog# 23225). Protein samples of equal concentrations were denatured by using NuPAGE™ 10X Reducer and LDS Sample Buffer (4X) (Thermo Fisher, Catalog No. NP0004, NP0007) as per the manufacturer’s instructions. Then 10 µg (retinal protein for albumin detection) or 35 µg (cell protein for phospho-JAK1 detection) was loaded on 10% acrylamide gels. Proteins were transferred to PVDF membranes (Immun-Blot, Bio-Rad Laboratory, Hercules, CA, USA), using the wet transfer method. Membranes were blocked with 5% Bovine Serum Albumin (Sigma-Aldrich, Catalog No. A3803) for 1 h, before primary antibody incubation overnight. The next day, membranes were washed, incubated in appropriate secondary antibody washed and developed by using Clarity Western ECL Blotting Substrate (Bio-Rad, Catalog No. 1705061). Membranes were imaged by using G:BOX Chemi XRQ chemiluminescence imager (Syngene, Cambridge, UK). Secondary antibody probing was used to confirm successful stripping. Densitometry was analyzed by using FIJI software.

Byrne E.M., Llorián-Salvador M., Tang M., Margariti A., Chen M, & Xu H. (2021). IL-17A Damages the Blood–Retinal Barrier through Activating the Janus Kinase 1 Pathway. Biomedicines, 9(7), 831.

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