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Genegnome xrq imaging system

Manufactured by Syngene
Sourced in United Kingdom

The GeneGnome XRQ imaging system is a high-performance, automated imaging platform designed for scientific research applications. It features a compact design, advanced optics, and a user-friendly interface to capture and analyze images of various biological samples, including gels, blots, and microplates. The GeneGnome XRQ provides researchers with a reliable and efficient tool for their imaging needs.

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6 protocols using genegnome xrq imaging system

1

Western Blot Analysis of Protein Expression

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After the required treatments, cells were washed with PBS, followed by lysis in RIPA buffer, and the sample buffer for SDS–PAGE was added. The protein concentrations were determined using the Pierce™ BCA Protein Assay Kit (Life Technologies Ltd, Paisley, UK). 20 μg protein per lane were separated by 10% SDS–PAGE and transferred to polyvinylidene difluoride membranes (Millipore, Billerica, MA, USA). Antibodies used were as follows listed in Supplementary Table S1.
Membranes were developed in a GeneGnome XRQ imaging system (Syngene, Cambridge, UK) with BM Chemiluminescence Western Blotting Substrate (POD) (Roche, Welwyn Garden City, UK).
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2

Phospho-Kinase Array in Prostate Cancer

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For the Proteome Profiler Human Phospho-Kinase Array (R&D, Abingdon, UK) 1 × 106 primary PCa cells were seeded in a collagen I-coated 10 cm-well plate and treated with 48 h-conditioned media from STO-IL-4 or STO-GUS for 30 min or 48 h. The array was performed according to the manufacturer’s manual and developed in a GeneGnome XRQ imaging system (Syngene, Cambridge, UK).
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3

Western Blot Analysis of Immune Signaling

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Protein samples were obtained from macrophages and glioblastoma cells. The processes of Western blot were consistent with previously reported [20 (link)]. Immunoreactions were visualized with a GeneGnome XRQ Imaging System (Syngene, UK). Primary antibodies utilized in our research were as follows: STAT3 (AF6294, Affinity), p-STAT3(YP0251, Immunoway), STAT1 (YT4439, Immunoway), p-STAT1 (YP0249, Immunoway), SIRPα (YT4301, Immunoway), CD47 (YT5509, Immunoway), β-actin (TA-09, ZSGB-BIO), and GAPDH (BA2913, BOSTER).
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4

Western Blot Analysis of RARRES2 in GBM

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Protein samples were obtained from normal brain tissue and IDH(Mut) and IDH(WT) GBM tissues. Next, the BCA Protein Assay kit (Beyotime) was used to determine the protein concentrations. Then, the protein lysates were separated by SDS‒PAGE electrophoresis. Then, the proteins were transferred to PVDF membranes and blocked in 5% skim milk followed by overnight incubation with primary antibodies at 4 °C. The membranes were rinsed and incubated with secondary antibodies for 1 h at room temperature. The GeneGnome XRQ Imaging System (Syngene, UK) was used to observe immunoreactivity. The following primary antibodies were used in this study: anti-RARRES2 (Cat#10216–1-AP Proteintech China) and anti-β-actin (Cat#66009–1-Ig Proteintech China).
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5

Evaluating the Impact of HYAL2 Knockdown on Glioma Cell Lines

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U251 and LN229 cell lines were treated with siHYAL2 for 48 h. Then, the glioma cells were lysed in RIPA solution on ice for 30 min. Next, total protein was extracted from glioma cell lines. 12.5% SDS‒PAGE gels were used to separate protein samples, and then the protein samples were transferred to PVDF membranes. After routinely blocking the membranes and incubating them with the primary and secondary antibodies, the GeneGnome XRQ Imaging System (Syngene, UK) was used to observe the immunoreactions. The primary antibodies were as follows: anti-HYAL2 (DF13080, Affinity); anti-CCND1 (26939-1-AP, Proteintech); anti-CCNB1 (28603-1-AP, Proteintech); anti-Bcl-2 (60178-1-Ig, Proteintech); anti-BAX (50599-2-Ig, Proteintech); and anti-β-actin (TA-09, ZSGB-BIO).
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6

Evaluating ATP7B Regulation via Western Blot

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Western blot analysis of ATP7B was performed as described previously (Pai et al. 2008) . In brief, snap frozen liver tissues from rats (n ¼ 4) treated orally for 14 days either with vehicle or GNE-470 at 50 and 150 mg/kg were homogenized in modified Radioimmunoprecipitation assay buffer (RIPA) containing protease and phosphatase inhibitors (Roche Diagnostics, Sigma-Aldrich, Thermo Scientifics, IL) and clarified by centrifugation. Total protein concentrations of the lysates were determined using bicinchoninic acid assay (Pierce, Rockford, IL) and equal amounts of protein (50 μg) were resolved on sodium dodecyl sulfate polyacrylamide gel electrophoresis transferred to nitrocellulose membranes and incubated with ATP7B-specific primary antibody (Novus Biologicals, Littleton, CO). After washing and incubating with secondary antibody, immunoreactive protein was visualized by the Enhanced Chemiluminescence (ECL) detection system (GE Healthcare, Buckinghamshire, United Kingdom) and imaged using GeneGnome XRQ imaging system (Syngene, Frederick, MD).
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