Image studio v3

Manufactured by LI COR

Sourced in United States, United Kingdom

Image Studio v3.1 is a software application developed by LI-COR for image analysis and quantification. It provides tools for visualizing, processing, and analyzing digital images. The software supports a variety of image file formats and enables users to perform basic image manipulation tasks such as adjusting brightness, contrast, and color levels.

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Lab products found in correlation

Odyssey blocking buffer, by LI COR (4 mentions) Odyssey sa infrared imaging system, by LI COR (4 mentions) Ktaprime plus system, by GE Healthcare (2 mentions) Imac sepharose 6 fast flow, by GE Healthcare (2 mentions) Irdye 800, by LI COR (2 mentions) Irdye 700, by LI COR (2 mentions) Odyssey image scanner system, by LI COR (2 mentions) Odyssey clx, by LI COR (1 mentions) Anti nap1l1, by Santa Cruz Biotechnology (1 mentions) Anti α actin, by Merck Group (1 mentions) Supersignal west femto maximum sensitivity substrate, by Thermo Fisher Scientific (1 mentions) Bca assay, by Thermo Fisher Scientific (1 mentions) Chemidoc xr, by Bio-Rad (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions) M7 pb e9, by Santa Cruz Biotechnology (1 mentions) α actin, by Merck Group (1 mentions) Odyssey fc, by LI COR (1 mentions) Mtor mab 7c10, by Cell Signaling Technology (1 mentions) Gfp d5.1 mab, by Cell Signaling Technology (1 mentions) Hrp conjugated donkey anti rabbit igg, by Jackson ImmunoResearch (1 mentions)

Close spelling variants of this product

Image Studio (447 citations) Image Studio™ Lite V3.1 (6 citations) Image Studio Digits v3.1 software (2 citations)

22 protocols using image studio v3

Plasmin(ogen) Binding Assay in T Cells

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The 0.1 × 10⁶ polyclonal T cells were incubated in 100 μl Accell medium containing 2 mM GlutaMAX-1, supplemented with 10 ng/ml IL-7 with 10 nM or 100 nM plasmin or plasminogen for 2 h.
Following incubation, the cells were washed with warm AIM-V medium three times before being centrifuged, and the supernatant was removed. The cell pellet was directly lysed in 62.5 μM Tris–HCl pH 6.8, 2% SDS, 10% glycerol, 5% β-mercaptoethanol, and 0.002% bromophenol blue at 95 °C for 5 min. Protein samples were fractionated on 12% SDS-PAGE gel and analyzed by Western blotting using antiplasminogen (Invitrogen) and anti-b-actin (A00702-100, GenScript) antibodies. Western blots were visualized using 680RD donkey antimouse (Li-Cor Biosciences) and 800 CW donkey anti-rabbit secondary antibodies (Li-Cor Biosciences) and an Odyssey CLx (Li-Cor Biosciences) dual-color imaging system. Quantitation of plasmin(ogen) binding was done using Image Studio v3.1 (Li-Cor Biosciences).

Loef E.J., Sheppard H.M., Birch N.P, & Dunbar P.R. (2022). Plasminogen and plasmin can bind to human T cells and generate truncated CCL21 that increases dendritic cell chemotactic responses. The Journal of Biological Chemistry, 298(7), 102112.

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Quantitative Western Blot Analysis

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Cells were washed twice in PBS, lysed in 1× Glasgow lysis buffer (GLB; 1% [vol/vol] Triton X-100, 120 mM KCl, 30 mM NaCl, 5 mM MgCl₂, 10% [vol/vol] glycerol, and 10 mM PIPES-NaOH, [pH 7.2], with protease and phosphatase inhibitors) and harvested by centrifugation (2,800 × g, 10 min, and 4°C) before determination and normalization of protein concentration by bicinchoninic acid (BCA) assay (Pierce). Following separation by SDS-PAGE, proteins were transferred to a polyvinylidene difluoride (PVDF) membrane and blocked in 50% (vol/vol) Odyssey blocking (OB) buffer (LI-COR) in Tris-buffered saline (TBS). The membrane was incubated with primary antibodies overnight at 4°C, followed by secondary antibodies for 2 h at room temperature, both prepared in 25% OB buffer. Primary antibodies used were anti-NS5A (sheep, prepared in-house) at 1:4,000 (52 (link)), anti-NAP1L1 (rabbit; Santa Cruz) at 1:350, anti-Bin1 (rabbit; Generon) at 1:300, anti-VAP-A (rabbit; Generon) at 1:1,000, anti-VAP-B (rabbit; Generon) at 1:1,000, and anti-α-actin (mouse; Sigma) at 1:10,000. Secondary antibodies were anti-rabbit, anti-sheep (800 nm), or anti-mouse (700 nm) antibodies, used at 1:10,000 prior to imaging using a LI-COR Odyssey Sa infrared imaging system. Quantification of Western blots was carried out using Image Studio v3.1 (LI-COR) using a background subtraction method.

Goonawardane N., Gebhardt A., Bartlett C., Pichlmair A, & Harris M. (2017). Phosphorylation of Serine 225 in Hepatitis C Virus NS5A Regulates Protein-Protein Interactions. Journal of Virology, 91(17), e00805-17.

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Western Blot Analysis of HCV Proteins

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Cells were washed twice in PBS, lysed in 1× Glasgow lysis buffer [GLB; 1 % (v/v) Triton X-100, 120 mM KCl, 30 mM NaCl, 5 mM MgCl₂, 10 % (v/v) glycerol, 10 mM PIPES-NaOH, pH 7.2, with protease and phosphatase inhibitors] and harvested by centrifugation (2800 g, 10 min, 4 °C) before determining and normalizing protein concentration by BCA assay (Pierce). Following separation by SDS-PAGE, proteins were transferred to a polyvinylidene difluoride (PVDF) membrane and blocked in 50 % (v/v) Odyssey blocking (OB) buffer (LI-COR) in PBS. The membrane was incubated with primary antibodies overnight at 4 °C, followed by secondary antibodies for 2 h at room temperature, both prepared in 50 % OB buffer. The primary antibodies used were: anti-NS5A (sheep), 1 : 5000 [34 (link)]; anti-NS3 (mouse), 1 : 2 000; and anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, mouse), 1 : 20 000 (Sigma). The secondary antibodies were anti-goat (800 nm) or anti-mouse (700 nm), used at 1 : 10 000 prior to imaging fluorescence using a LI-COR Odyssey Sa infrared imaging system. Quantification of fluorescently labelled Western blots were carried out using Image Studio v3.1 (LI-COR) using a background subtraction method.

Goonawardane N., Yin C, & Harris M. (2019). Phenotypic analysis of mutations at residue 146 provides insights into the relationship between NS5A hyperphosphorylation and hepatitis C virus genome replication. The Journal of General Virology, 101(3), 252-264.

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Quantitative Fluorescence Imaging of Tumors

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Imaging data was randomized and regions of interest (ROIs) were drawn in a blinded fashion. ROIs were drawn around core tumor area and tumor margins for tissue slices in Image Studio v. 3.1 (LI-COR) according to H&E validation of tumor location (Fig. 1). To compare average standard deviation of mean fluorescence intensity (MFI) for each agent, large ROIs were drawn (Fig. 1B). To compare average TBRs for Fig. 4, smaller ROIs (n = 3 for each variable in Eqns. 1-3), were drawn (Fig. 1B). To compare between groups, shown in Fig. 5, ROIs shown in Fig. 1A were drawn.
Proximal background fluorescence measurements were taken close to the tumor margin. Distal background fluorescence measurements were taken at the edge of the brain as far away from the tumor as possible. All fluorescence signal is reported in arbitrary units (a.u). H&E stains were used to determine true tumor.

Napier T.S., Udayakumar N., Jani A.H., Hartman Y.E., Houson H.A., Moore L., Amm H.M., van den Berg N.S., Sorace A.G, & Warram J.M. (2020). Comparison of Panitumumab-IRDye800CW and 5-Aminolevulinic Acid to Provide Optical Contrast in a Model of Glioblastoma Multiforme. Molecular cancer therapeutics, 19(9), 1922-1929.

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Protein Quantification and Visualization

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Protein content in samples was measured using the BCA assay (Thermo Scientific). Proteins were fractionated on 10% Mini-PROTEAN TGX gels and transferred to PVDF membranes (Bio-Rad). Membranes were blocked in 5% milk and incubated with the following primary antibodies: rabbit α-HCN1 (3 µg/mL), rabbit α-TRIP8b (1∶10,000), mouse α-NKA (M7-PB-E9, Santa Cruz, 1∶1000), rabbit α-PDC (gift from Dr. Maxim Sokolov, 1∶3000) and secondary antibodies conjugated to HRP. Blots were incubated with SuperSignal West Femto Maximum Sensitivity Substrates (Thermo Scientific) and visualized with a CCD camera (ChemiDoc XR+, Bio-Rad). The software package Image Studio v3.1 (LI-COR Biosciences) was used for analysis of the images.

Pan Y., Bhattarai S., Modestou M., Drack A.V., Chetkovich D.M, & Baker S.A. (2014). TRIP8b Is Required for Maximal Expression of HCN1 in the Mouse Retina. PLoS ONE, 9(1), e85850.

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Quantitative Western Blot Analysis

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Cells were washed twice in PBS, lysed in 1x Glasgow lysis buffer (GLB – 1 % (v/v) Triton X-100, 120 mM KCl, 30 mM NaCl, 5 mM MgCl₂, 10 % (v/v) glycerol, 10 mM PIPES-NaOH, pH 7.2 with protease and phosphatase inhibitors) and harvested by centrifugation (2800 g, 10 min, 4 °C) before determining and normalizing protein concentration by BCA assay (Pierce). Following separation by SDS-PAGE, proteins were transferred to a polyvinylidene difluoride (PVDF) membrane and blocked in 50 % (v/v) Odyssey blocking (OB) buffer (LI-COR) in Tris-buffered saline (TBS). The membrane was incubated with primary antibodies overnight at 4 °C, followed by secondary antibodies for 2 h at room temperature, both prepared in 25 % OB buffer. Primary antibodies used were; anti-NS5A (sheep, prepared in-house, 1 : 4000) and α-Actin (mouse, Sigma, 1 : 10 000). Secondary antibodies were anti-sheep (800 nm) or anti-mouse (700 nm), used at 1 : 10 000 prior to imaging using a LI-COR Odyssey Sa infrared imaging system. Quantification of Western blots was carried out using Image Studio v3.1 (LI-COR) using a background subtraction method.

Goonawardane N., Ross-Thriepland D, & Harris M. (2017). Regulation of hepatitis C virus replication via threonine phosphorylation of the NS5A protein. The Journal of General Virology, 99(1), 62-72.

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Protein Quantification in T Cells

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Equal amounts of cell lysate proteins from sorted T cells were resolved on 12% SDS-PAGE, and transferred onto PVDF membranes using standard procedures. Primary antibodies were as follows: mTOR mAb (7C10), phospho-p70 S6 kinase (Thr389) (108D2) mAb, phospho-AKT (Ser473) (D9E) mAb, and GFP (D5.1) mAb (Cell Signaling Technology). The secondary antibody was HRP-conjugated Donkey-anti-Rabbit IgG (Jackson ImmunoResearch). Data were imaged by Odyssey Fc (Li-Cor) and protein bands were analyzed by densitometry using Image Studio V3.1 (Li-Cor).

Chen W., Wan X., Ukah T.K., Miller M.M., Barik S., Cattin-Roy A.N, & Zaghouani H. (2016). Antigen-Specific Immune Modulation Targets mTORC1 Function to Drive Chemokine Receptor-Mediated T Cell Tolerance. Journal of immunology (Baltimore, Md. : 1950), 197(9), 3554-3565.

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Qm1 Protein Purification from SHuffle T7 Express E. coli

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For the Qm1 purification from SHuffle^® T7 Express E. coli, the cells were resuspended in PBS buffer and lysed by a mechanical disruption in an EmulsiFlex C-5 High-pressure homogenizer from Avestin (Ottawa, ON, Canada) and centrifuged at 17,500× g for 10 min at 4 °C to separate the pellet of the soluble fraction. The soluble fraction was loaded onto a Ni²⁺ charged column IMAC SepharoseTM 6 Fast Flow, connected to an ÄKTA prime plus system, both from GE Healthcare (Chicago, IL, USA). The column was equilibrated with five column volumes (CVs) of PBS buffer, then the sample was loaded and the flow-through was collected for analysis. The elution was made using Imidazole in PBS buffer at increasing concentrations: 25, 50, 150, and 400 mM (Supplementary Material, Figure S3). The purified Qm1 protein was quantified by SDS-PAGE by densitometry using bovine serum albumin as an external standard. The images were captured and processed using the LI-COR Odyssey imaging system program Image Studio v 3.1 (LI-COR, USA).

Lamazares E., Gutiérrez F., Hidalgo A., Gutiérrez N.A., Espinoza F.I., Sánchez O., Cortez-San Martín M., Mascayano C., González J., Saavedra J., Altamirano C., Mansur M., Ruiz Á, & Toledo J.R. (2020). A Heterologous Viral Protein Scaffold for Chimeric Antigen Design: An Example PCV2 Virus Vaccine Candidate. Viruses, 12(4), 385.

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Purification of Soluble epIL-18 by IMAC

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Soluble epIL-18 was purified by immobilized metal affinity chromatography (IMAC). The soluble fraction from E. coli rupture was loaded into a Ni²⁺ charged matrix IMAC SepharoseTM 6 Fast Flow (GE Healthcare, Chicago, IL, USA), connected to the GE ÄKTA prime plus system. The decreasing urea gradient (8 to 0 M) was completed to recover not-denaturing conditions. Elution was performed with increasing imidazole concentration (25, 250, and 500 mM). Purified epIL-18 was quantified by SDS-PAGE using bovine serum albumin as an external standard and the recovery percentage of the initial fraction was calculated by densitometry. Images were captured and processed using an LI-COR imaging system program (Image Studio v 3.1, LI-COR, Lincoln, NE, USA).

Hidalgo-Gajardo A., Gutiérrez N., Lamazares E., Espinoza F., Escobar-Riquelme F., Leiva M.J., Villavicencio C., Mena-Ulecia K., Montesino R., Altamirano C., Sánchez O., Rivas C.I., Ruíz Á, & Toledo J.R. (2023). Co-Formulation of Recombinant Porcine IL-18 Enhances the Onset of Immune Response in a New Lawsonia intracellularis Vaccine. Vaccines, 11(12), 1788.

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Quantitative Western Blot Analysis

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Western blots were quantified using LI-COR Image Studio v3.1 software (LI-COR). After subtracting background, quantified bands were normalized to quantified β-actin band in the same lane on the same membrane. n, discussed in figure legends, represents biological replicates of a given experiment; error bars represent SEM.

Porter J.R., Fisher B.E., Baranello L., Liu J.C., Kambach D.M., Nie Z., Koh W.S., Luo J., Stommel J.M., Levens D, & Batchelor E. (2017). Global inhibition with specific activation: how p53 and MYC redistribute the transcriptome in the DNA double-strand break response. Molecular cell, 67(6), 1013-1025.e9.

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