iodoacetamide Search Results


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  • 99
    Thermo Fisher iodoacetamide iam
    <t>Iodoacetamide</t> ( IAM ) labelling of C5a CF proofs the existence of only one free cysteine residue. (A) C5a CF containing an N‐terminal 6xHis tag and TEV cleavage site is detected in MALDI ‐ TOF at 11583 Da corresponding to the theoretical molecular weight of 11582 Da. (B) Labelling with 0.1 m m IAM does not result in any mass shift of the protein. (C and D) Labelling with 1 m m and 10 m m IAM sequentially shifts the molecular weight of C5a CF towards 11640 Da corresponding to a 57 Da mass shift expected for one accessible sulphydryl group. Nonspecific side reactions are not observed as no additional peaks at higher molecular weight are detected with increasing concentrations of IAM .
    Iodoacetamide Iam, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore iodoacetamide iam
    A limited set of higher-confidence identifications can be created using differential covalent modification to flag cysteine-containing peptides. (A) Comparison of rabbit CCH spectra from samples treated with <t>iodoacetamide</t> (Cys +57 Da) vs iodoethanol (Cys +44 Da) results in a 13 Da mass difference per cysteine. PSMs for paired spectra exhibiting a mass shift but no cysteine residues in the corresponding matched sequences can be flagged as false identifications. (B) Comparison of precursor mass offsets between differentially labeled rabbit CCH samples confirms alkylation and oxidation account for the most abundant modifications.
    Iodoacetamide Iam, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 752 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad iodoacetamide iam
    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of <t>iodoacetamide</t> (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed
    Iodoacetamide Iam, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare iodoacetamide iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Sinopharm iodoacetamide iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Millipore mass spectrometry iodocetamide iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
    Mass Spectrometry Iodocetamide Iam, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tokyo Chemical Industry iam iodoacetamide
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
    Iam Iodoacetamide, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Eppendorf AG iodoacetamide iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Millipore biotin iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
    Biotin Iam, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore iodoacetamide iaa
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
    Iodoacetamide Iaa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1071 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OlChemIm n iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Regis Technologies iam column
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Regis Technologies iam particles
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Roche iodoacetomide iam
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    Amresco iodoacetamide
    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 <t>C]iodoacetamide,</t> separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).
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    FUJIFILM iam
    Identification of indole compounds produced by ectomycorrhizal fungi using high performance liquid chromatography technique. A. Indole compounds standard, B. Uncultivated liquid medium. C. Crude culture extract of Astraeus odoratus . D. Crude culture extract of Gyrodon suthepensis . E. crude culture extract of Phlebopus portentosus . F. Crude culture extract of Pisolithus albus . G. Crude culture extract of Pisolithus orientalis . H. crude culture extract of Scleroderma suthepense . L-Trp = L-tryptophan, TAM = tryptamine, <t>IAM</t> = indole-3-acetamide, ILA = indole-3-lactic acid, IPyA = indole-3-pyruvic acid, <t>IAA</t> = indole-3-acetic acid, IOL = indole-3-ethanol and IAN = indole-3-acetonitrile. The analyses were performed in triplicate.
    Iam, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck & Co iodoacetamide
    Identification of indole compounds produced by ectomycorrhizal fungi using high performance liquid chromatography technique. A. Indole compounds standard, B. Uncultivated liquid medium. C. Crude culture extract of Astraeus odoratus . D. Crude culture extract of Gyrodon suthepensis . E. crude culture extract of Phlebopus portentosus . F. Crude culture extract of Pisolithus albus . G. Crude culture extract of Pisolithus orientalis . H. crude culture extract of Scleroderma suthepense . L-Trp = L-tryptophan, TAM = tryptamine, <t>IAM</t> = indole-3-acetamide, ILA = indole-3-lactic acid, IPyA = indole-3-pyruvic acid, <t>IAA</t> = indole-3-acetic acid, IOL = indole-3-ethanol and IAN = indole-3-acetonitrile. The analyses were performed in triplicate.
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    Merck KGaA iodoacetamide
    Identification of indole compounds produced by ectomycorrhizal fungi using high performance liquid chromatography technique. A. Indole compounds standard, B. Uncultivated liquid medium. C. Crude culture extract of Astraeus odoratus . D. Crude culture extract of Gyrodon suthepensis . E. crude culture extract of Phlebopus portentosus . F. Crude culture extract of Pisolithus albus . G. Crude culture extract of Pisolithus orientalis . H. crude culture extract of Scleroderma suthepense . L-Trp = L-tryptophan, TAM = tryptamine, <t>IAM</t> = indole-3-acetamide, ILA = indole-3-lactic acid, IPyA = indole-3-pyruvic acid, <t>IAA</t> = indole-3-acetic acid, IOL = indole-3-ethanol and IAN = indole-3-acetonitrile. The analyses were performed in triplicate.
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    Valiant iodoacetamide
    B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. <t>Iodoacetamide,</t> a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P
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    Thermo Fisher iodoacetamide alkyne
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    Dojindo Labs iodoacetamide
    B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. <t>Iodoacetamide,</t> a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P
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    Molecular Biosciences Inc β 4 hydroxyphenyl ethyl iodoacetamide hpe iam
    B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. <t>Iodoacetamide,</t> a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P
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    Avantor iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Cambridge Isotope Laboratories iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Supelco iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    BioShop iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Fisher Scientific iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Applichem iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Nacalai iodoacetamide
    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with <t>iodoacetamide</t> and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.
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    Image Search Results


    Iodoacetamide ( IAM ) labelling of C5a CF proofs the existence of only one free cysteine residue. (A) C5a CF containing an N‐terminal 6xHis tag and TEV cleavage site is detected in MALDI ‐ TOF at 11583 Da corresponding to the theoretical molecular weight of 11582 Da. (B) Labelling with 0.1 m m IAM does not result in any mass shift of the protein. (C and D) Labelling with 1 m m and 10 m m IAM sequentially shifts the molecular weight of C5a CF towards 11640 Da corresponding to a 57 Da mass shift expected for one accessible sulphydryl group. Nonspecific side reactions are not observed as no additional peaks at higher molecular weight are detected with increasing concentrations of IAM .

    Journal: FEBS Open Bio

    Article Title: Cell‐free synthesis of isotopically labelled peptide ligands for the functional characterization of G protein‐coupled receptors

    doi: 10.1002/2211-5463.12008

    Figure Lengend Snippet: Iodoacetamide ( IAM ) labelling of C5a CF proofs the existence of only one free cysteine residue. (A) C5a CF containing an N‐terminal 6xHis tag and TEV cleavage site is detected in MALDI ‐ TOF at 11583 Da corresponding to the theoretical molecular weight of 11582 Da. (B) Labelling with 0.1 m m IAM does not result in any mass shift of the protein. (C and D) Labelling with 1 m m and 10 m m IAM sequentially shifts the molecular weight of C5a CF towards 11640 Da corresponding to a 57 Da mass shift expected for one accessible sulphydryl group. Nonspecific side reactions are not observed as no additional peaks at higher molecular weight are detected with increasing concentrations of IAM .

    Article Snippet: Iodoacetamide‐labelling assay About 5–10 μg C5aCF or ET‐1CF (both in their respective buffers CC5a or CET−1 from purification) were labelled with 0.1 mm , 1 mm and 10 mm iodoacetamide (Thermo Scientific) for 15 min at RT.

    Techniques: Molecular Weight

    ET ‐1 CF does not contain free cysteine residues and can be fully processed by furin protease. (A) Full‐length ET ‐1 CF is detected at 6980 Da and is presumably formylated at the N‐terminal methionine residue (mass addition of 27 Da). (B) Upon treatment with furin, the peptide peak at 6980 Da can no longer be observed, indicating a complete processing of the peptide precursor. Consistently, a signal at 2493 Da corresponding to the cleaved peptide ( pET ‐1 CF ) can be detected in furin‐treated fET ‐1 CF but not in uncleaved pET ‐1 CF (insets in B and A respectively). (C) Treatment of fET ‐1 CF with 10 m m iodoacetamide does not shift the molecular mass of the peptide, demonstrating that no free cysteine residues are present in the peptide.

    Journal: FEBS Open Bio

    Article Title: Cell‐free synthesis of isotopically labelled peptide ligands for the functional characterization of G protein‐coupled receptors

    doi: 10.1002/2211-5463.12008

    Figure Lengend Snippet: ET ‐1 CF does not contain free cysteine residues and can be fully processed by furin protease. (A) Full‐length ET ‐1 CF is detected at 6980 Da and is presumably formylated at the N‐terminal methionine residue (mass addition of 27 Da). (B) Upon treatment with furin, the peptide peak at 6980 Da can no longer be observed, indicating a complete processing of the peptide precursor. Consistently, a signal at 2493 Da corresponding to the cleaved peptide ( pET ‐1 CF ) can be detected in furin‐treated fET ‐1 CF but not in uncleaved pET ‐1 CF (insets in B and A respectively). (C) Treatment of fET ‐1 CF with 10 m m iodoacetamide does not shift the molecular mass of the peptide, demonstrating that no free cysteine residues are present in the peptide.

    Article Snippet: Iodoacetamide‐labelling assay About 5–10 μg C5aCF or ET‐1CF (both in their respective buffers CC5a or CET−1 from purification) were labelled with 0.1 mm , 1 mm and 10 mm iodoacetamide (Thermo Scientific) for 15 min at RT.

    Techniques: Positron Emission Tomography

    A limited set of higher-confidence identifications can be created using differential covalent modification to flag cysteine-containing peptides. (A) Comparison of rabbit CCH spectra from samples treated with iodoacetamide (Cys +57 Da) vs iodoethanol (Cys +44 Da) results in a 13 Da mass difference per cysteine. PSMs for paired spectra exhibiting a mass shift but no cysteine residues in the corresponding matched sequences can be flagged as false identifications. (B) Comparison of precursor mass offsets between differentially labeled rabbit CCH samples confirms alkylation and oxidation account for the most abundant modifications.

    Journal: Analytical Chemistry

    Article Title: Proteomic Identification of Monoclonal Antibodies from Serum

    doi: 10.1021/ac4037679

    Figure Lengend Snippet: A limited set of higher-confidence identifications can be created using differential covalent modification to flag cysteine-containing peptides. (A) Comparison of rabbit CCH spectra from samples treated with iodoacetamide (Cys +57 Da) vs iodoethanol (Cys +44 Da) results in a 13 Da mass difference per cysteine. PSMs for paired spectra exhibiting a mass shift but no cysteine residues in the corresponding matched sequences can be flagged as false identifications. (B) Comparison of precursor mass offsets between differentially labeled rabbit CCH samples confirms alkylation and oxidation account for the most abundant modifications.

    Article Snippet: Incomplete Freund’s Adjuvant (IFA), TRIS hydrocholoride (Tris-HCl), ammonium bicarbonate (NH4 HCO3 ), 2,2,2-trifluoroethanol (TFE), dithiothrietol (DTT), triethylphosphine (TEP), iodoacetamide (IAM), and iodoethanol (IE) were obtained from Sigma-Aldrich (St. Louis, MO).

    Techniques: Modification, Labeling

    Effect of iodoacetamide pretreatment in wild-type mice

    Journal:

    Article Title: Deletion of the acid-sensing ion channel ASIC3 prevents gastritis-induced acid hyperresponsiveness of the stomach – brainstem axis

    doi: 10.1016/j.pain.2007.04.025

    Figure Lengend Snippet: Effect of iodoacetamide pretreatment in wild-type mice

    Article Snippet: To induce gastritis, iodoacetamide (Sigma, Vienna, Austria) was added to the drinking water at a concentration of 0.1 % (w/w) for 7 days ( ; ).

    Techniques: Mouse Assay

    Control of MIMOOX folding. A , oxidation of MIMOOX was verified in HPLC method between T = 0 h ( dashed line ) and T = 6 h ( continuous line ). B , mass spectrometry after alkylation with iodoacetamide of MIMO ( black ), MIMOOX in oxidation conditions at T =

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Highly Conserved Surface on Tat Variants *

    doi: 10.1074/jbc.M113.466011

    Figure Lengend Snippet: Control of MIMOOX folding. A , oxidation of MIMOOX was verified in HPLC method between T = 0 h ( dashed line ) and T = 6 h ( continuous line ). B , mass spectrometry after alkylation with iodoacetamide of MIMO ( black ), MIMOOX in oxidation conditions at T =

    Article Snippet: MIMO and MIMOOX outlines were compared with HPLC analysis, and the oxidation (disulfide bridge formation) was controlled by alkylation assays using 85 m m iodoacetamide (Sigma).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry

    Metallothionein N-terminal peptides are susceptible to methionine oxidation. Cytosol from untreated HK-2(MT3) cells (800 μg) was alkylated with 14 N-iodoacetamide. An internal standard of 206 pmol 15 N-MT-3 peptide was added. The cytosol was digested

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Quantitation of Human Metallothionein Isoforms: A Family of Small, Highly Conserved, Cysteine-rich Proteins *

    doi: 10.1074/mcp.M113.033373

    Figure Lengend Snippet: Metallothionein N-terminal peptides are susceptible to methionine oxidation. Cytosol from untreated HK-2(MT3) cells (800 μg) was alkylated with 14 N-iodoacetamide. An internal standard of 206 pmol 15 N-MT-3 peptide was added. The cytosol was digested

    Article Snippet: 15 N-iodoacetamide was obtained from Sigma-Aldrich (St. Louis, MO).

    Techniques:

    The 14 N- and 15 N-labeled N-terminal MT peptides have similar chromatographic and ionization properties. Equal amounts of cytosols from Cd 2+ -induced HK-2(MT3) cells were alkylated with 14 N- or 15 N-iodoacetamide, combined, and digested with trypsin. The

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Quantitation of Human Metallothionein Isoforms: A Family of Small, Highly Conserved, Cysteine-rich Proteins *

    doi: 10.1074/mcp.M113.033373

    Figure Lengend Snippet: The 14 N- and 15 N-labeled N-terminal MT peptides have similar chromatographic and ionization properties. Equal amounts of cytosols from Cd 2+ -induced HK-2(MT3) cells were alkylated with 14 N- or 15 N-iodoacetamide, combined, and digested with trypsin. The

    Article Snippet: 15 N-iodoacetamide was obtained from Sigma-Aldrich (St. Louis, MO).

    Techniques: Labeling

    Iodoacetamide and DNFB do not target myofilament proteins

    Journal: The Journal of Physiology

    Article Title: Synergistic role of ADP and Ca2+ in diastolic myocardial stiffness

    doi: 10.1113/JP270354

    Figure Lengend Snippet: Iodoacetamide and DNFB do not target myofilament proteins

    Article Snippet: Specifically, 5 m m fresh iodoacetamide (I6125, Sigma) was dissolved in Tyrode buffer and perfused (at 1 ml min−1 ) for 3 min, delivering a total dose of 15 μmol (3 ml)−1 .

    Techniques:

    Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of iodoacetamide (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed

    Journal: Plant Physiology

    Article Title: Glutamine Synthetase Is a Molecular Target of Nitric Oxide in Root Nodules of Medicago truncatula and Is Regulated by Tyrosine Nitration 1 and Is Regulated by Tyrosine Nitration 1 [W] and Is Regulated by Tyrosine Nitration 1 [W] [OA]

    doi: 10.1104/pp.111.186056

    Figure Lengend Snippet: Effects of modifications on Cys and Tyr residues on the activity of MtGS1a and MtGS2a. Purified MtGS1a or MtGS2a was treated with increasing concentrations of iodoacetamide (A), S-GSNO (B), hydrogen peroxide (C), or N -acetyl imidazole (D) and assayed

    Article Snippet: TNM, S-GSNO, and SNP were obtained from Sigma; epicatechin and N -acetyl-imidazole were from Fluka; and iodocetamide was from Bio-Rad.

    Techniques: Activity Assay, Purification

    Effects of iodoacetamide on MtGS1a inactivation induced by TNM and PN. Purified MtGS1a was treated with 500 μ m iodoacetamide, followed by incubation with 50 μ m PN or 50 μ m TNM at pH 8, and assayed for GS activity. GS activity was

    Journal: Plant Physiology

    Article Title: Glutamine Synthetase Is a Molecular Target of Nitric Oxide in Root Nodules of Medicago truncatula and Is Regulated by Tyrosine Nitration 1 and Is Regulated by Tyrosine Nitration 1 [W] and Is Regulated by Tyrosine Nitration 1 [W] [OA]

    doi: 10.1104/pp.111.186056

    Figure Lengend Snippet: Effects of iodoacetamide on MtGS1a inactivation induced by TNM and PN. Purified MtGS1a was treated with 500 μ m iodoacetamide, followed by incubation with 50 μ m PN or 50 μ m TNM at pH 8, and assayed for GS activity. GS activity was

    Article Snippet: TNM, S-GSNO, and SNP were obtained from Sigma; epicatechin and N -acetyl-imidazole were from Fluka; and iodocetamide was from Bio-Rad.

    Techniques: Purification, Incubation, Activity Assay

    The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 C]iodoacetamide, separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).

    Journal: Molecular and Cellular Biology

    Article Title: Molecular Architecture of the Human Prp19/CDC5L Complex ▿Molecular Architecture of the Human Prp19/CDC5L Complex ▿ †

    doi: 10.1128/MCB.01505-09

    Figure Lengend Snippet: The native human Prp19/CDC5L complex contains four copies of hPrp19. (A) Determination of the protein stoichiometry by fluorescence staining. Four different amounts of hPrp19/CDC5L complex proteins (as indicated above each lane) were separated by SDS gel electrophoresis and stained with Sypro-Ruby. The fluorescence was detected by fluorescence imaging (FLA-7000; Fujifilm). (B) Determination of the protein stoichiometry by radioactive labeling. Denatured proteins (0.5 to 12.5 μg, as indicated) were labeled with [ 14 C]iodoacetamide, separated by SDS-PAGE and detected by autoradiography. (C) Band intensities obtained after Sypro-Ruby staining and [ 14 C]iodoacetamide labeling were quantified using Fuji Image Gauge v4.22 and normalized against the CDC5L signal. (D) Continuous size distribution [C (S) ] analysis of the hPrp19/CDC5L complex. Four different concentrations of the complex were analyzed (optical densities at 280 nm [OD 280 ] of 1.2, 0.6, 0.3, and 0.15) as indicated in the figure. The calculated C (S) is plotted against the sedimentation coefficient (S). The S values in the panel are corrected according to standard conditions [S (20,w) ]. (E) Multispeed sedimentation equilibrium analysis of the hPrp19/CDC5L complex at two different rotor speeds (gray, 5,500 rpm; black, 3,500 rpm). The OD 280 values along the cell were recorded and are shown in the upper panel. The lower panel shows the residuals between the fit (straight line in the upper panel) and the raw data (dots in the upper panel).

    Article Snippet: Subsequently, the pH was increased to 9.0 with 100 mM Tris-HCl buffer, and [14 C]iodoacetamide (56 mCi/mmol; GE Healthcare) was added to a concentration of 50 mM.

    Techniques: Fluorescence, Staining, SDS-Gel, Electrophoresis, Imaging, Labeling, SDS Page, Autoradiography, Sedimentation

    Identification of indole compounds produced by ectomycorrhizal fungi using high performance liquid chromatography technique. A. Indole compounds standard, B. Uncultivated liquid medium. C. Crude culture extract of Astraeus odoratus . D. Crude culture extract of Gyrodon suthepensis . E. crude culture extract of Phlebopus portentosus . F. Crude culture extract of Pisolithus albus . G. Crude culture extract of Pisolithus orientalis . H. crude culture extract of Scleroderma suthepense . L-Trp = L-tryptophan, TAM = tryptamine, IAM = indole-3-acetamide, ILA = indole-3-lactic acid, IPyA = indole-3-pyruvic acid, IAA = indole-3-acetic acid, IOL = indole-3-ethanol and IAN = indole-3-acetonitrile. The analyses were performed in triplicate.

    Journal: PLoS ONE

    Article Title: Biosynthetic pathway of indole-3-acetic acid in ectomycorrhizal fungi collected from northern Thailand

    doi: 10.1371/journal.pone.0227478

    Figure Lengend Snippet: Identification of indole compounds produced by ectomycorrhizal fungi using high performance liquid chromatography technique. A. Indole compounds standard, B. Uncultivated liquid medium. C. Crude culture extract of Astraeus odoratus . D. Crude culture extract of Gyrodon suthepensis . E. crude culture extract of Phlebopus portentosus . F. Crude culture extract of Pisolithus albus . G. Crude culture extract of Pisolithus orientalis . H. crude culture extract of Scleroderma suthepense . L-Trp = L-tryptophan, TAM = tryptamine, IAM = indole-3-acetamide, ILA = indole-3-lactic acid, IPyA = indole-3-pyruvic acid, IAA = indole-3-acetic acid, IOL = indole-3-ethanol and IAN = indole-3-acetonitrile. The analyses were performed in triplicate.

    Article Snippet: Rf values were individually determined for the standards of L-Trp, IAA (Sigma-Aldrich, Germany, Cat No. I-2886,), IAM (Wako Pure Chemicals, Japan, Cat No. 325–42383), indole-3-lactic acid (ILA; Wako Pure Chemicals, Japan, Cat No. 325–45301), IAN (Sigma-Aldrich, Germany, Cat No. 129453), indole-3-ethanol (IOL; Wako Pure Chemicals, Japan, Cat No. 350–15601,), IPyA (Sigma-Aldrich, Germany, Cat No. I-17017) and TAM (Sigma-Aldrich, Germany, Cat No. 193747) under UV light (254 nm).

    Techniques: Produced, High Performance Liquid Chromatography

    B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. Iodoacetamide, a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P

    Journal: Eukaryotic Cell

    Article Title: Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿

    doi: 10.1128/EC.00371-07

    Figure Lengend Snippet: B. ratti WR1 exposure to intestinal epithelial cells causes IκB-α degradation and induces NF-κB activation. (A) Live WR1 parasite or lysate coincubation with T84 cells resulted in IκB-α degradation at 5 h, as shown in a representative result with a β-actin loading conrol. The cell lysates were analyzed by Western blotting using an anti-IκB-α antibody. Pretreatment of the cells with the NF-κB inhibitor BAY11-7082 resulted in decreased IκB-α degradation. Iodoacetamide, a cysteine protease inhibitor, decreased the WR1 lysate-induced degradation of IκB-α. The histogram represents densitometry values expressed as arbitrary units ± standard deviations (SD). (B) A representative EMSA shows NF-κB/IL-8 promoter binding activity in nuclear extracts of T84 cells coincubated with WR1 lysate for 6 h. No NF-κB/DNA binding was observed in a mutant NF-κB oligoduplex incubated with nuclear extract, a wild-type NF-κB oligoduplex without nuclear extract, and the control. Pretreatment of T84 cells with the NF-κB inhibitor BAY11-7082 resulted in decreased WR1-induced NF-κB/DNA binding. (C) Histogram showing the increase in NF-κB activity in nuclear extracts of T84 cells. The cells were coincubated with WR1 lysate for 6 h, and NF-κB activity was measured by specific ELISA. The values are means ± SD ( n = 3). *, P

    Article Snippet: All inhibitors were purchased from Sigma except pepstatin A (Chemicon), iodoacetamide (MP Biomedicals, LLC), and PMSF (BDH).

    Techniques: Activation Assay, Western Blot, Protease Inhibitor, Binding Assay, Activity Assay, Mutagenesis, Incubation, Enzyme-linked Immunosorbent Assay

    Protease activity of B. ratti WR1 and cellular localization of cysteine proteases. (A) Protease activity was determined with azocasein as a substrate. Lysates from 4 × 10 6 parasites were used for each sample. The assay was performed with and without protease inhibitors as described in Materials and Methods. Significant inhibition of protease activity could be noticed with cysteine protease inhibitors (iodoacetamide and E-64), and less significant inhibition was seen with the aspartic inhibitor pepstatin A. The metalloprotease inhibitor EDTA and the serine inhibitor PMSF showed no inhibition. One azocasein unit was defined as the amount of enzyme producing an increase of 0.01 optical density units/h. The values are means ± standard deviations ( n = 3). #, P

    Journal: Eukaryotic Cell

    Article Title: Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿

    doi: 10.1128/EC.00371-07

    Figure Lengend Snippet: Protease activity of B. ratti WR1 and cellular localization of cysteine proteases. (A) Protease activity was determined with azocasein as a substrate. Lysates from 4 × 10 6 parasites were used for each sample. The assay was performed with and without protease inhibitors as described in Materials and Methods. Significant inhibition of protease activity could be noticed with cysteine protease inhibitors (iodoacetamide and E-64), and less significant inhibition was seen with the aspartic inhibitor pepstatin A. The metalloprotease inhibitor EDTA and the serine inhibitor PMSF showed no inhibition. One azocasein unit was defined as the amount of enzyme producing an increase of 0.01 optical density units/h. The values are means ± standard deviations ( n = 3). #, P

    Article Snippet: All inhibitors were purchased from Sigma except pepstatin A (Chemicon), iodoacetamide (MP Biomedicals, LLC), and PMSF (BDH).

    Techniques: Activity Assay, Inhibition

    Effects of protease inhibitors on IL-8 production from T84 cells induced by B. ratti WR1. T84 cells were coincubated for 24 h with WR1 lysate pretreated with one of several protease inhibitors. Cysteine protease inhibitors, iodoacetamide and E-64, most significantly reduced WR1-induced IL-8 production from T84 cells (*, P = 0.002, and **, P = 0.007, versus WR1 lysate). Considerable reduction in IL-8 production was seen with the aspartic inhibitor pepstatin A (##, P = 0.04 versus WR1 lysate). Minimal inhibition was observed with serine and metalloprotease inhibitors, PMSF and EDTA, respectively. The values are means ± standard deviations ( n = 3). #, P

    Journal: Eukaryotic Cell

    Article Title: Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿

    doi: 10.1128/EC.00371-07

    Figure Lengend Snippet: Effects of protease inhibitors on IL-8 production from T84 cells induced by B. ratti WR1. T84 cells were coincubated for 24 h with WR1 lysate pretreated with one of several protease inhibitors. Cysteine protease inhibitors, iodoacetamide and E-64, most significantly reduced WR1-induced IL-8 production from T84 cells (*, P = 0.002, and **, P = 0.007, versus WR1 lysate). Considerable reduction in IL-8 production was seen with the aspartic inhibitor pepstatin A (##, P = 0.04 versus WR1 lysate). Minimal inhibition was observed with serine and metalloprotease inhibitors, PMSF and EDTA, respectively. The values are means ± standard deviations ( n = 3). #, P

    Article Snippet: All inhibitors were purchased from Sigma except pepstatin A (Chemicon), iodoacetamide (MP Biomedicals, LLC), and PMSF (BDH).

    Techniques: Inhibition

    B. ratti WR1 induces up-regulation of IL-8 mRNA levels in T84 cells. T84 cells were coincubated with live WR1 parasites or parasite lysate for 12 h. Total cellular RNA was isolated, and IL-8 and β-actin mRNA levels were measured by quantitative real-time RT-PCR as described in Materials and Methods. WR1 lysate caused a significant increase in IL-8 mRNA levels. A significant decrease in IL-8 mRNA levels was noticed after treatment with the NF-κB inhibitor BAY11-7082 and the cysteine protease inhibitor iodoacetamide. The increase in IL-8 mRNA relative to untreated T84 cells was calculated for each experiment based on internal β-actin controls. The values are means ± standard deviations ( n = 3). *, P

    Journal: Eukaryotic Cell

    Article Title: Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an NF-?B-Dependent Manner ▿

    doi: 10.1128/EC.00371-07

    Figure Lengend Snippet: B. ratti WR1 induces up-regulation of IL-8 mRNA levels in T84 cells. T84 cells were coincubated with live WR1 parasites or parasite lysate for 12 h. Total cellular RNA was isolated, and IL-8 and β-actin mRNA levels were measured by quantitative real-time RT-PCR as described in Materials and Methods. WR1 lysate caused a significant increase in IL-8 mRNA levels. A significant decrease in IL-8 mRNA levels was noticed after treatment with the NF-κB inhibitor BAY11-7082 and the cysteine protease inhibitor iodoacetamide. The increase in IL-8 mRNA relative to untreated T84 cells was calculated for each experiment based on internal β-actin controls. The values are means ± standard deviations ( n = 3). *, P

    Article Snippet: All inhibitors were purchased from Sigma except pepstatin A (Chemicon), iodoacetamide (MP Biomedicals, LLC), and PMSF (BDH).

    Techniques: Isolation, Quantitative RT-PCR, Protease Inhibitor

    High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with iodoacetamide and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.

    Journal: Biochemistry

    Article Title: High-Throughput Assay for Collagen Secretion Suggests an Unanticipated Role for Hsp90 in Collagen Production

    doi: 10.1021/acs.biochem.8b00378

    Figure Lengend Snippet: High-throughput screening strategy and results. (A) Schematic of screen design. Addition of 1 μg/mL doxycycline (Dox) to the stable single-colony Saos-2 GLuc.Col cell line induces expression of the eGLuc2.Colα2(I) fusion protein, which can be proteolytically processed post-secretion. Luminescence generated by the fusion protein may be assayed upon addition of the eGLuc2 substrate. (B) eGLuc2.Colα2(I) from Saos-2 GLuc.Col lysate was immunoprecipitated with an α-GLuc antibody and analyzed by immunoblotting, revealing that eGLuc2.Colα2(I) associates intracellularly with Colα1(I). (C) Disulfide-dependent assembly of eGLuc2.Colα2(I) with Colα1(I). Collagen-I precipitated from conditioned media of Saos-2 GLuc.Col cells was treated with iodoacetamide and heated in Laemmli buffer with or without DTT. Samples were separated by SDS-PAGE and analyzed by immunoblotting. (D) Plot of filtered screening results. (E) Validated small molecule modulators of collagen-I secretion.

    Article Snippet: After reduction, samples were cooled at rt for 15 min, and then 4.28 μL of 600 mM iodoacetamide (IAA; VWR) in NaHCO3 buffer was added to yield a final concentration of 60 mM.

    Techniques: High Throughput Screening Assay, Expressing, Generated, Immunoprecipitation, SDS Page