Imagequant las 4010

Manufactured by GE Healthcare

Sourced in United States, United Kingdom, Japan

The ImageQuant LAS 4010 is a high-performance, automated lab equipment that is used for the detection and quantification of various biomolecules, such as proteins and nucleic acids, in Western blots and other gel-based assays. It utilizes a charge-coupled device (CCD) camera and advanced imaging technology to capture high-quality images of chemiluminescent, fluorescent, and colorimetric signals.

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Lab products found in correlation

Laemmli sample buffer, by Bio-Rad (5 mentions) Hybond, by Cytiva (4 mentions) Enhanced chemi luminescence (ecl), by Merck Group (3 mentions) Pvdf membrane, by Roche (3 mentions) Imagequant tl, by GE Healthcare (3 mentions) Image studio lite version 5, by LI COR (2 mentions) Polyvinylidene fluoride membrane, by Merck Group (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Cell lysis buffer, by Cell Signaling Technology (2 mentions) Proteome profiler human phospho rtk array kit, by R&D Systems (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Nuclear and cytoplasmic protein extraction kit, by Beyotime (2 mentions) Enhanced chemiluminescence solution, by Thermo Fisher Scientific (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Blocking one, by Nacalai Tesque (2 mentions) Dig luminescent detection kit, by Roche (2 mentions) Hybond n, by Roche (2 mentions) Pcr dig probe synthesis kit, by Roche (2 mentions) Ab213363, by Abcam (2 mentions)

Spelling variants of this product

ImageQuant (354 citations) ImageQuant LAS 4010 imager (14 citations) ImageQuant LAS 4010 system (9 citations) ImageQuant LAS 4010 Imaging System (6 citations) ImageQuant LAS 4010 CCD camera (4 citations) ImageQuant LAS 4010 camera system (3 citations) ImageQuant LAS 4010 Digital Imaging System (2 citations) ImageQuant LAS 4010 Control Software (2 citations)

80 protocols using imagequant las 4010

Quantifying Soluble and Insoluble Fractions of TAMRA-labeled Protein

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TAMRA-labeled 13A in a solution containing 0.2% Triton X-100 and 25 mM EDTA was centrifuged at 22,000 g at 4°C for 30 min as essentially described [32 (link)]. The resultant supernatant was collected as the soluble fraction. Then, the pellet was re-dissolved with a same volume of a solution containing 2% SDS and 25 mM EDTA as the insoluble fraction.
One microliter of each fraction was dropped onto PVDF membrane pre-soaked with methanol. The TAMRA signal was detected by ImageQuant^TM LAS 4010 (GE Healthcare, Chalfont Saint Giles, UK). Mean signal intensity and the area of the signal were measured using Image J software and were multiplied to yield the amount of 13A in each fraction. Percentages of the amounts of 13A in insoluble fractions relative to the amounts in soluble fractions were calculated.

Okumura H., Itoh S.G., Zen H, & Nakamura K. (2023). Dissociation process of polyalanine aggregates by free electron laser irradiation. PLOS ONE, 18(9), e0291093.

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Western Blotting Protein Analysis

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Western blotting was performed as previously described^{59 (link)}. Primary antibodies were used at 1:1000 except anti-GAPDH at 1:2000. Western blotting data were analysed using ImageQuant^TM LAS4010 (GE Healthcare).

Sato N., Yako Y., Maruyama T., Ishikawa S., Kuromiya K., Tokuoka S.M., Kita Y, & Fujita Y. (2020). The COX-2/PGE2 pathway suppresses apical elimination of RasV12-transformed cells from epithelia. Communications Biology, 3, 132.

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Western Blot Analysis of TFEB and mTOR Signaling

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Equal amounts of proteins from U87-MG cell lysates (30 μg of proteins) were mixed with Laemmli solution, run in 4–15% polyacrylamide gels (Mini-PROTEAN^® Precast Gels, Biorad, Hercules, CA, USA) using a mini-Protean Tetracell (Biorad, Hercules, CA, USA), and transferred onto nitrocellulose membranes (0.2 μm) using a Trans-Blot Turbo transfer system (Biorad) as previously described [33 (link)]. Immediately after, WB membranes were stained with 1 mM RuBP and total protein images acquired by ImageQuant LAS4010 (GE Health Care, Uppsala, Sweden). Subsequently, membranes were incubated with primary antibodies (dilution 1:1000). The following antibodies were purchased from Cell Signaling Technology, Beverly, MA, USA: TFEB (D207D) rabbit mAb (#37785), phosphorylated TFEB (E9S8N) rabbit mAb (pTFEBS211; #37681), mTOR (7C10) rabbit mAb (#2983), phosphorylated mTOR (D9C2) XP rabbit mAb (p-mTORS2448; #5536). Immunoblots were developed using the enhanced chemiluminescence (ECL) detection system. The chemiluminescent images were acquired using LAS4010 (GE Health Care Europe, Upsala, Sweden). Semiquantitative analysis of specific immunolabeled bands was performed using ImageQuant TL 7 software.

Polini B., Zallocco L., Gado F., Ferrisi R., Ricardi C., Zuccarini M., Carnicelli V., Manera C., Ronci M., Lucacchini A., Zucchi R., Giusti L, & Chiellini G. (2024). A Proteomic Approach Identified TFEB as a Key Player in the Protective Action of Novel CB2R Bitopic Ligand FD22a against the Deleterious Effects Induced by β-Amyloid in Glial Cells. Cells, 13(10), 875.

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Profiling Kinase Phosphorylation in J-Lat Cells

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Proteome profiler human phospho-kinase arrays were purchased from R&D Systems, Inc. (Minneapolis, MN, United States). Ten million J-Lat 5A8 cells were treated for 30 min with 200 nM rGal-9 or an equivalent volume of PBS. Cells were washed twice in cold PBS and processed according to the manufacturer's instructions. Briefly, the cells were lysed for 30 min on a rotating shaker at 4°C. Lysates were centrifuged at 14,000 g for 5 min, and supernatants were incubated on the array membrane overnight on an orbital shaker at 4°C. Membranes were washed three times and incubated for 2 h at room temperature with anti-horseradish peroxidase antibody. After another three washes, membranes were incubated for 1 min with Chemi Reagent. Membrane images were captured using ImageQuant LAS 4010 (GE Healthcare Bio-Sciences, Pittsburg, PA, United States) and densitometry analysis was performed with Image Studio Lite Version 5.2 (LI-COR Biotechnology, Lincoln, NE, United States).

Colomb F., Giron L.B., Premeaux T.A., Mitchell B.I., Niki T., Papasavvas E., Montaner L.J., Ndhlovu L.C, & Abdel-Mohsen M. (2019). Galectin-9 Mediates HIV Transcription by Inducing TCR-Dependent ERK Signaling. Frontiers in Immunology, 10, 267.

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Detailed Research Equipment Specifications

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The Spectrophotometer Zenyth 200 (ELISA reader) was from Anthos (Eugendorf, Austria).

The Kinematica Polytron was from Brinkmann Instruments (Westbury, NY, USA).

The flow cytometer used was the FACSCalibur, including its software, from Becton Dickinson (Mountain View, CA, USA).

The Elisa reader Ceres UV 900 was from Bio-Tek (Burlington, VT, USA).

The β-counter, a 1600 CA Tri-Carb liquid scintillation analyzer, was from Packard (Meriden, CT, USA).

Surgery equipment was from Bar Naor (Ramat-Gan, Israel).

The densitometric apparatus was ImageQuant LAS 4010 (GE Health Care Life Sciences, Rehovot, Israel).

Thermal cycler (MJ Mini, Bio-Rad Laboratories, Rishon Le Zion, Israel).

E-Gel PowerBase apparatus (Invitrogen, Life Technologies, RHENIUM, Modi'in, Israel)

LAS-3000 luminescent image analyzer (Fujifilm, Tokyo, Japan).

Hamilton–Kinder sensor in a soundproof ventilated apparatus (Kinder Scientific, Poway, CA, USA).

Z1 inverted microscope (Zeiss, Oberkochen, Germany).

Vainshtein A., Veenman L., Shterenberg A., Singh S., Masarwa A., Dutta B., Island B., Tsoglin E., Levin E., Leschiner S., Maniv I., Pe’er L., Otradnov I., Zubedat S., Aga-Mizrachi S., Weizman A., Avital A., Marek I, & Gavish M. (2015). Quinazoline-based tricyclic compounds that regulate programmed cell death, induce neuronal differentiation, and are curative in animal models for excitotoxicity and hereditary brain disease. Cell Death Discovery, 1, 15027-.

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In Vitro Binding Assay for CLASP2-N2 and PAR3-2N

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The in vitro binding assay was performed as described previously (Watanabe et al., 2009 (link)). Briefly, purified MBP-tagged CLASP2-N2 was mixed with affinity beads coated with GST–PAR3-2N in buffer A. The beads were then washed with buffer A, and the bound proteins were eluted with buffer A containing 10 mM reduced glutathione. The eluates were subjected to SDS–PAGE, followed by immunoblot analysis using an anti-MBP antibody. The amount of CLASP2-N2 bound to GST-PAR3-2N was detected in a linear range using serial dilutions of standards by chemiluminescent detection and estimated with a Densitograph (ATTO, Tokyo, Japan) or with the ImageQuant LAS 4010 (GE Healthcare Bio-Sciences). Purified CLASP2-N2 was used as the standard for quantification.

Matsui T., Watanabe T., Matsuzawa K., Kakeno M., Okumura N., Sugiyama I., Itoh N, & Kaibuchi K. (2015). PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity. Molecular Biology of the Cell, 26(4), 751-761.

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Western Blot Analysis of Protein Markers

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Whole cell lysates were prepared in RIPA buffer and were subjected to Western blot analyses as previously described 7. Proteins on the PVDF membranes were probed with antibodies against EGFR (C13, BD Biosciences, San Jose, CA), P‐EGFR (Tyr1068), P‐EGFR (Tyr1173), Akt, P‐Akt (Thr308), P‐Akt (Ser473), P‐mammalian target of rapamycin (mTOR) (Ser2448), mTOR (Cell Signaling, Danvers, MA), O⁶‐methylguanine‐DNA methyltransferase (MGMT) (MT3.1, Neo Markers, Fremont, CA), MSH6, MLH1, MSH2, PMS2 (BD Biosciences), detected by chemiluminescence, and quantified (ImageQuant LAS4010, GE Healthcare, Tokyo, Japan). Loading of lysates on membranes was evaluated by β‐actin blot or Ponceau S staining (St. Louis, MO, Sigma‐Aldrich).

Nitta Y., Shimizu S., Shishido‐Hara Y., Suzuki K., Shiokawa Y, & Nagane M. (2016). Nimotuzumab enhances temozolomide‐induced growth suppression of glioma cells expressing mutant EGFR in vivo. Cancer Medicine, 5(3), 486-499.

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Soft Agar Assay for Cisplatin Sensitivity

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For the soft agar assay, 1 ml of bottom agar (0.5% agar/RPMI or DMEM + 10% FBS) and 1 ml of top agar (0.33% agar/RPMI or DMEM + 10% FBS) were plated on 6-well plates (n = 3) with or without cisplatin (0.125 μM, 0.5 μM, 2 μM, and 8 μΜ, respectively). Negative control or NCAN-overexpressing cells (4,000 YT-nu, TNB1 or NB39 cells) were seeded into the top agar. Two weeks later, the colonies were stained with crystal violet and counted with an ImageQuant LAS-4010 digital imaging system (GE Healthcare).

Su Z., Kishida S., Tsubota S., Sakamoto K., Cao D., Kiyonari S., Ohira M., Kamijo T., Narita A., Xu Y., Takahashi Y, & Kadomatsu K. (2017). Neurocan, an extracellular chondroitin sulfate proteoglycan, stimulates neuroblastoma cells to promote malignant phenotypes. Oncotarget, 8(63), 106296-106310.

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Protein Extraction and Western Blot Analysis

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The total proteins (100 µg) were extracted using protein lysates containing protease inhibitors and were resolved in 10% sodium dodecyl sulfate (SDS)‐poly‐acrylamide gels and transferred electrophoretically to polyvinylidene fluoride (PVDF) membranes. 5% skim milk was used to block the PVDF membranes and dilute the primary antibodies (Table S2, Supporting Information). The blots were then incubated with the corresponding secondary antibody and visualized by enhanced chemiluminescence using ImageQuant LAS4010 (GE Healthcare).

Liu S., Cheng K., Zhang H., Kong R., Wang S., Mao C, & Liu S. (2020). Methylation Status of the Nanog Promoter Determines the Switch between Cancer Cells and Cancer Stem Cells. Advanced Science, 7(5), 1903035.

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Acetylated Protein Detection by Western Blot

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Proteins separated by 1-D and 2-DE gel electrophoresis were transferred onto nitrocellulose membranes (0.2 mm). Immediately after WB, the membranes were fixed in 7% acetic acid (v/v) and 10% methanol (v/v) for 15 min, subsequently rinsed with H₂O, and stained with 1 mM RuBP (SunaTech Inc.; Suzhou, P. R. China) in 1% phosphoric acid and 30% ethanol for 15 min. Membranes were then rinsed with H₂O prior to the acquisition of the total proteins by “ImageQuant LAS4010” (GE HealthCare). After acquisition, membranes were blocked with 3% low fat dried milk, 0.2% (v/v) Tween 20 in PBS for 1 h at room temperature. Subsequently, membranes were incubated 2 h at room temperature with the primary antibody for acetylated-lysine (mouse monoclonal; 1:1,000 dilution, Cell Signaling Technology Inc., MA, USA). HRP-conjugated goat antimouse (1:10,000 dilution; PerkinElmer, MA, USA) was used as a secondary antibody. Immunoblots were developed using the ECL detection system (PerkinElmer, MA, USA). The chemiluminescent images were acquired by “ImageQuant LAS4010”.

Ciregia F., Bugliani M., Ronci M., Giusti L., Boldrini C., Mazzoni M.R., Mossuto S., Grano F., Cnop M., Marselli L., Giannaccini G., Urbani A., Lucacchini A, & Marchetti P. (2017). Palmitate-induced lipotoxicity alters acetylation of multiple proteins in clonal β cells and human pancreatic islets. Scientific Reports, 7, 13445.

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