li cor odyssey scanner  (LI-COR)


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    Structured Review

    LI-COR li cor odyssey scanner
    Li Cor Odyssey Scanner, supplied by LI-COR, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/li cor odyssey scanner/product/LI-COR
    Average 99 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    li cor odyssey scanner - by Bioz Stars, 2020-04
    99/100 stars

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    Related Articles

    Marker:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Transfection:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Labeling:

    Article Title: FOXC1 negatively regulates BMP-SMAD activity and Id1 expression during osteoblast differentiation.
    Article Snippet: Bone morphogenetic proteins regulate a diverse range of biological processes through their activation of SMAD1, SMAD5, or SMAD8 proteins that, in turn, regulate gene expression. .. Bone morphogenetic proteins regulate a diverse range of biological processes through their activation of SMAD1, SMAD5, or SMAD8 proteins that, in turn, regulate gene expression.

    Concentration Assay:

    Article Title: FOXC1 negatively regulates BMP-SMAD activity and Id1 expression during osteoblast differentiation.
    Article Snippet: Bone morphogenetic proteins regulate a diverse range of biological processes through their activation of SMAD1, SMAD5, or SMAD8 proteins that, in turn, regulate gene expression. .. Bone morphogenetic proteins regulate a diverse range of biological processes through their activation of SMAD1, SMAD5, or SMAD8 proteins that, in turn, regulate gene expression.

    Incubation:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Electrophoretic Mobility Shift Assay:

    Article Title: FOXC1 negatively regulates BMP-SMAD activity and Id1 expression during osteoblast differentiation.
    Article Snippet: Paragraph title: 2.5 | Electrophoretic mobility shift assay ... Bone morphogenetic proteins regulate a diverse range of biological processes through their activation of SMAD1, SMAD5, or SMAD8 proteins that, in turn, regulate gene expression.

    Western Blot:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Sequencing:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Sonication:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Lysis:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade. .. The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

    Binding Assay:

    Article Title: Yorkie Growth-Promoting Activity Is Limited by Atg1-Mediated Phosphorylation.
    Article Snippet: Paragraph title: Yki Binding Assays ... The expression of multiple growth-promoting genes is coordinated by the transcriptional co-activator Yorkie with its major regulatory input provided by the Hippo-Warts kinase cascade.

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    LI-COR li cor odyssey scanner
    Ub B stimulates cIAP1R-catalyzed Ub transfer. A , nonreduced autoradiograms of lysine discharge reactions showing the disappearance of UbcH5B variant∼ 32 P-Ub over time in the presence and absence of UbΔGG (300 μ m ) catalyzed by cIAP1R. B , nonreduced SDS-PAGE showing the cIAP1R-mediated discharge of <t>fluorescently</t> labeled UbcH5B∼Ub to l -lysine over time in the presence of UbΔGG (20 μ m ) or UbcH5B S22R,F62A,P95D–Ub (20 μ m ) visualized with a <t>LI-COR</t> Odyssey scanner ( top ) followed by staining with InstantBlue ( bottom ). *, fluorescently labeled Ub.
    Li Cor Odyssey Scanner, supplied by LI-COR, used in various techniques. Bioz Stars score: 99/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/li cor odyssey scanner/product/LI-COR
    Average 99 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    li cor odyssey scanner - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

    Image Search Results


    Ub B stimulates cIAP1R-catalyzed Ub transfer. A , nonreduced autoradiograms of lysine discharge reactions showing the disappearance of UbcH5B variant∼ 32 P-Ub over time in the presence and absence of UbΔGG (300 μ m ) catalyzed by cIAP1R. B , nonreduced SDS-PAGE showing the cIAP1R-mediated discharge of fluorescently labeled UbcH5B∼Ub to l -lysine over time in the presence of UbΔGG (20 μ m ) or UbcH5B S22R,F62A,P95D–Ub (20 μ m ) visualized with a LI-COR Odyssey scanner ( top ) followed by staining with InstantBlue ( bottom ). *, fluorescently labeled Ub.

    Journal: The Journal of Biological Chemistry

    Article Title: Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B∼ubiquitin complex

    doi: 10.1074/jbc.RA118.006045

    Figure Lengend Snippet: Ub B stimulates cIAP1R-catalyzed Ub transfer. A , nonreduced autoradiograms of lysine discharge reactions showing the disappearance of UbcH5B variant∼ 32 P-Ub over time in the presence and absence of UbΔGG (300 μ m ) catalyzed by cIAP1R. B , nonreduced SDS-PAGE showing the cIAP1R-mediated discharge of fluorescently labeled UbcH5B∼Ub to l -lysine over time in the presence of UbΔGG (20 μ m ) or UbcH5B S22R,F62A,P95D–Ub (20 μ m ) visualized with a LI-COR Odyssey scanner ( top ) followed by staining with InstantBlue ( bottom ). *, fluorescently labeled Ub.

    Article Snippet: Fluorescently labeled UbcH5B∼Ub was visualized by a LI-COR Odyssey scanner, followed by staining with InstantBlue.

    Techniques: Variant Assay, SDS Page, Labeling, Staining

    Addition of N-linked oligosaccharide at fourth position does not change efficiency of amino-terminal tripeptide-enhanced GH trafficking. (A) Chemical structure of N-linked glycosylation on APVNTT peptide (amino-terminal alanine at top). (B) Western blot: GH starting with high-efficiency motif, APV, obtained lower steady-state levels in HEK293A cells compared to same protein starting with predicted nonbinding motif, EET. Addition of N-linked oligosaccharide (NTT motif inserted at position 4) caused PNGaseF-susceptible increases in size (M r ) but did not change relative trafficking efficiencies of either strong (APV-NTT) or nonbinding (EET-NTT) proteins. The oligosaccharides on cell layer–associated GH by both constructs were removed by Endo H digestion, showing no Golgi modifications. Cells and media were collected 16 hr posttransfection. Three μg of cell lysate or 6% of concentrated media was used for western blot analysis with goat anti-human GH. LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner. Numbers on left are molecular weight standards in kDa. APV, alanine-proline-valine; EET, glutamic acid–glutamic acid–threonine; GH, growth hormone; HEK293A, human embryonic kidney cell line 293A; IR, infrared; NTT, asparagine-threonine-threonine.

    Journal: PLoS Biology

    Article Title: Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum

    doi: 10.1371/journal.pbio.2005140

    Figure Lengend Snippet: Addition of N-linked oligosaccharide at fourth position does not change efficiency of amino-terminal tripeptide-enhanced GH trafficking. (A) Chemical structure of N-linked glycosylation on APVNTT peptide (amino-terminal alanine at top). (B) Western blot: GH starting with high-efficiency motif, APV, obtained lower steady-state levels in HEK293A cells compared to same protein starting with predicted nonbinding motif, EET. Addition of N-linked oligosaccharide (NTT motif inserted at position 4) caused PNGaseF-susceptible increases in size (M r ) but did not change relative trafficking efficiencies of either strong (APV-NTT) or nonbinding (EET-NTT) proteins. The oligosaccharides on cell layer–associated GH by both constructs were removed by Endo H digestion, showing no Golgi modifications. Cells and media were collected 16 hr posttransfection. Three μg of cell lysate or 6% of concentrated media was used for western blot analysis with goat anti-human GH. LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner. Numbers on left are molecular weight standards in kDa. APV, alanine-proline-valine; EET, glutamic acid–glutamic acid–threonine; GH, growth hormone; HEK293A, human embryonic kidney cell line 293A; IR, infrared; NTT, asparagine-threonine-threonine.

    Article Snippet: LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner.

    Techniques: Western Blot, Construct, Molecular Weight

    Erv29p is critical for trafficking of DSPP and PRY-family proteins in S . cerevisiae . (A) Immunoblot of wild-type DSPP Flag (IPV) or DSPP Flag starting with the mutant tripeptide motif (IPD) in α or erv29 Δ cell lysates. Yeast α or erv29 Δ cells were transformed with pYES expression plasmid encoding IPV- or IPD-DSPP Flag under GAL1 promoter and induced for 5 hr. For rescue experiments, pAG425GPD plasmid constitutively expressing Erv29p was cotransformed with DSPP-encoding plasmids. Note that IPV-DSPP Flag was well trafficked out of the ER/cells of wild-type α cells, while IPD-DSPP Flag protein was retained. The erv29 Δ cells could not efficiently traffic IPV-DSPP Flag protein unless it was cotransformed with Erv29p-expressing plasmid (rescue). Media contained Kex2-digested, Flag-tagged carboxy-terminal fragment DPP. Four μg of cell lysate protein and 10% of the concentrated conditioned media were used for Flag-tag detection on western blots. (B) Yeast wild-type α cells or erv29 Δ cells were transformed with pYES expression plasmids encoding Pry1p or Pry2p, each with 2xHA-tags near the amino-terminus. Five hr after induction, 30 μg of cell lysate protein was analyzed by western blots. For each construct, higher M r bands (solid red arrowheads) were proteins containing Golgi-acquired posttranslational modifications, while ER-retained proteins lack these modifications and electrophorese several kDa faster (open green arrowheads). Note both APA/APV and APD showed increases in the smaller ER forms in erv29Δ cells, while only APD shows abundance in ER forms in wild-type (α) cells. (C) Pry1p and Pry2p modified to express both 2xHA-tag (near amino-terminus) and Myc (carboxy-terminus) showed faster electrophoresing proteins (ER) were not due to endogenous protease activity. LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner. Numbers on left are molecular weight standards in kDa. APA, alanine-proline-alanine; APD, alanine-proline-aspartic acid; APV, alanine-proline-valine; DPP, dentin phosphoprotein; DSPP, dentin sialophosphoprotein; ER, endoplasmic reticulum; Erv29p, ER-derived vesicles protein 29; HA, hemagglutinin; IPD, isoleucine-proline-aspartic acid; IPV, isoleucine-proline-valine; IR, infrared; Kex2, kexin 2; PRY, pathogen-related yeast.

    Journal: PLoS Biology

    Article Title: Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum

    doi: 10.1371/journal.pbio.2005140

    Figure Lengend Snippet: Erv29p is critical for trafficking of DSPP and PRY-family proteins in S . cerevisiae . (A) Immunoblot of wild-type DSPP Flag (IPV) or DSPP Flag starting with the mutant tripeptide motif (IPD) in α or erv29 Δ cell lysates. Yeast α or erv29 Δ cells were transformed with pYES expression plasmid encoding IPV- or IPD-DSPP Flag under GAL1 promoter and induced for 5 hr. For rescue experiments, pAG425GPD plasmid constitutively expressing Erv29p was cotransformed with DSPP-encoding plasmids. Note that IPV-DSPP Flag was well trafficked out of the ER/cells of wild-type α cells, while IPD-DSPP Flag protein was retained. The erv29 Δ cells could not efficiently traffic IPV-DSPP Flag protein unless it was cotransformed with Erv29p-expressing plasmid (rescue). Media contained Kex2-digested, Flag-tagged carboxy-terminal fragment DPP. Four μg of cell lysate protein and 10% of the concentrated conditioned media were used for Flag-tag detection on western blots. (B) Yeast wild-type α cells or erv29 Δ cells were transformed with pYES expression plasmids encoding Pry1p or Pry2p, each with 2xHA-tags near the amino-terminus. Five hr after induction, 30 μg of cell lysate protein was analyzed by western blots. For each construct, higher M r bands (solid red arrowheads) were proteins containing Golgi-acquired posttranslational modifications, while ER-retained proteins lack these modifications and electrophorese several kDa faster (open green arrowheads). Note both APA/APV and APD showed increases in the smaller ER forms in erv29Δ cells, while only APD shows abundance in ER forms in wild-type (α) cells. (C) Pry1p and Pry2p modified to express both 2xHA-tag (near amino-terminus) and Myc (carboxy-terminus) showed faster electrophoresing proteins (ER) were not due to endogenous protease activity. LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner. Numbers on left are molecular weight standards in kDa. APA, alanine-proline-alanine; APD, alanine-proline-aspartic acid; APV, alanine-proline-valine; DPP, dentin phosphoprotein; DSPP, dentin sialophosphoprotein; ER, endoplasmic reticulum; Erv29p, ER-derived vesicles protein 29; HA, hemagglutinin; IPD, isoleucine-proline-aspartic acid; IPV, isoleucine-proline-valine; IR, infrared; Kex2, kexin 2; PRY, pathogen-related yeast.

    Article Snippet: LI-COR IR-fluorescent second antibodies were used for detection on LI-COR’s Odyssey scanner.

    Techniques: Mutagenesis, Transformation Assay, Expressing, Plasmid Preparation, FLAG-tag, Western Blot, Construct, Modification, Activity Assay, Molecular Weight, Derivative Assay

    NIR-mbc94 Binds to CB 2 Receptors Expressed by Intact Cells: Heterologous Expression (A) Saturation and competition of NIR-mbc94 binding to CB 2 receptors. Fluorescent signal emitted by increasing concentrations of NIR-mbc94 bound to CB 2 mid DBT cells was measured with a Li-Cor Odyssey scanner. Specific binding data are expressed as fluorescence values or relative functional units (RFU on the y axis) as a function of MI concentration (on the x axis). Data points for specific binding were obtained by subtracting the amount of fluorescence emitted by NIR-mbc94 incubated with CB 2 mid DBT cells minus fluorescence emitted by NIR-mbc94 incubated with untransfected DBT cells, using the values for corresponding concentrations. Inset shows these two curves. Data represent the mean ± SEM from three experiments, each performed in triplicate and on independent cell cultures. (B) Image of NIR-mbc94 bound to CB 2 receptors. Shown is a representative image of NIR-mbc94 (1 μM) bound to CB 2 mid DBT cells, gated to the fluorescent signal emitted by NIR-mbc94 bound to untransfected DBT cells image ( i.e. for detailed images). (C and D) Concentration-dependent competition of NIR-mbc94 bound to CB 2 receptors. CB 2 mid DBT cells were preincubated for 15 min with increasing concentrations of SR144528 (C) or WIN55212-2 (D), and then incubated for 30 min with NIR-mbc94 (200 nM). Fluorescence signal was measured with a Li-Cor Odyssey scanner. Data represent the mean ± SEM from at least three experiments, each performed in triplicate and on independent cell cultures. .

    Journal: Chemistry & biology

    Article Title: NIR-mbc94, a Fluorescent Ligand that Binds to Endogenous CB2 Receptors and Is Amenable to High-Throughput Screening

    doi: 10.1016/j.chembiol.2011.02.016

    Figure Lengend Snippet: NIR-mbc94 Binds to CB 2 Receptors Expressed by Intact Cells: Heterologous Expression (A) Saturation and competition of NIR-mbc94 binding to CB 2 receptors. Fluorescent signal emitted by increasing concentrations of NIR-mbc94 bound to CB 2 mid DBT cells was measured with a Li-Cor Odyssey scanner. Specific binding data are expressed as fluorescence values or relative functional units (RFU on the y axis) as a function of MI concentration (on the x axis). Data points for specific binding were obtained by subtracting the amount of fluorescence emitted by NIR-mbc94 incubated with CB 2 mid DBT cells minus fluorescence emitted by NIR-mbc94 incubated with untransfected DBT cells, using the values for corresponding concentrations. Inset shows these two curves. Data represent the mean ± SEM from three experiments, each performed in triplicate and on independent cell cultures. (B) Image of NIR-mbc94 bound to CB 2 receptors. Shown is a representative image of NIR-mbc94 (1 μM) bound to CB 2 mid DBT cells, gated to the fluorescent signal emitted by NIR-mbc94 bound to untransfected DBT cells image ( i.e. for detailed images). (C and D) Concentration-dependent competition of NIR-mbc94 bound to CB 2 receptors. CB 2 mid DBT cells were preincubated for 15 min with increasing concentrations of SR144528 (C) or WIN55212-2 (D), and then incubated for 30 min with NIR-mbc94 (200 nM). Fluorescence signal was measured with a Li-Cor Odyssey scanner. Data represent the mean ± SEM from at least three experiments, each performed in triplicate and on independent cell cultures. .

    Article Snippet: To measure the fluorescent signal emitted by NIR-mbc94, we used a LI-COR Odyssey scanner, which is suitable for HTS.

    Techniques: Expressing, Binding Assay, Fluorescence, Functional Assay, Concentration Assay, Incubation

    Scheme outlining a novel method to quantify cell migration with near-infrared fluorescence. ( a ) Primary mouse microglial cells were harvested from mixed glial cultures by shaking. ( b ) Microglia were resuspended in serum-free MEM and stained with DRAQ5 ( c ) Stained cells were loaded in upper wells of a 96-well Boyden Chamber, with chemoattractant solutions in the lower wells. The chamber was then incubated for three hours, allowing cells to migrate toward the chemoattractant. ( d ) After incubation, filter was removed from the chamber and non-migrated cells on the top of the filter were wiped off. The filter was then fixed in methanol. ( e ) Fluorescence signal emitted by cells that did migrate was scanned using a LI-COR Odyssey scanner.

    Journal: Glia

    Article Title: Microglial cell migration stimulated by ATP and C5a involve distinct molecular mechanisms

    doi: 10.1002/glia.20813

    Figure Lengend Snippet: Scheme outlining a novel method to quantify cell migration with near-infrared fluorescence. ( a ) Primary mouse microglial cells were harvested from mixed glial cultures by shaking. ( b ) Microglia were resuspended in serum-free MEM and stained with DRAQ5 ( c ) Stained cells were loaded in upper wells of a 96-well Boyden Chamber, with chemoattractant solutions in the lower wells. The chamber was then incubated for three hours, allowing cells to migrate toward the chemoattractant. ( d ) After incubation, filter was removed from the chamber and non-migrated cells on the top of the filter were wiped off. The filter was then fixed in methanol. ( e ) Fluorescence signal emitted by cells that did migrate was scanned using a LI-COR Odyssey scanner.

    Article Snippet: In the first part of our study, we presented evidence for the combined use of DRAQ5 and the LI-COR Odyssey scanner to reliably quantify cell migration when using a Boyden Chamber.

    Techniques: Migration, Fluorescence, Staining, Incubation