β mercaptoethanol  (Thermo Fisher)


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    Name:
    Gibco 2 Mercaptoethanol
    Description:
    Gibco 2 Mercaptoethanol also known as beta mercaptoethanol or BME is a potent reducing agent used in cell culture media to prevent toxic levels of oxygen radicals 2 Mercaptoethanol is not stable in solution so most protocols require daily supplementation Gibco 2 Mercaptoethanol contains 2 mercaptoethanol at a concentration of 55 mM in Dulbecco s phosphate buffered saline DPBS cGMP manufacturing and quality systemGibco Reducing Agent is manufactured at a cGMP compliant facility located in Grand Island New York The facility is registered with the FDA as a medical device manufacturer and is certified to ISO 13485 standards
    Catalog Number:
    21985023
    Price:
    None
    Applications:
    Cell Culture|Mammalian Cell Culture
    Category:
    Cell Culture Transfection Reagents
    Buy from Supplier


    Structured Review

    Thermo Fisher β mercaptoethanol
    ER-retention of APP by addition of the di-lysine motif KKAA induces SDS stable homo-dimers in an oxidizing cellular surrounding. a Schematic illustration of the APP domain structure and the used dilysine retention constructs. APP isoform 695 (APP695) was fused to a C-terminal myc-tag, followed by either a KKAA ER retention motif, or a “leaky” KKFF motif allowing trafficking to the cis -Golgi compartment. The E1 domain, acidic domain, E2 domain, transmembrane domain (TM), and the intracellular domain are indicated. b CHO-K1 cells stably over expressing the respective APP695 wt or APP695 retention constructs were subjected to cell surface biotinylation. To inhibit endocytosis from the cell surface, AP180 D/N (lane four) was transiently co-expressed. At 24-h post-transfection, cell surface proteins were labeled with sulfo NHS-SS-biotin at 4°C, prior to lysis. Biotinylated samples were precipitated with NeutrAvidin agarose beads and analyzed by SDS-PAGE and Western blot (PD: NeutrAvidin; right panel ). As input controls, 20 μg of cell lysates were used (input; left panel ). APP full length, CTFs and AP180 D/N were probed with 9E10 antibody. Monoclonal α-Tubulin antibody served as a loading control to verify the absence of endomembrane contaminants in the biotinylation. For the input control, all samples were treated with SDS sample loading buffer, containing <t>β-mercaptoethanol</t> (BME) without heat denaturing prior to SDS gel electrophoresis. To elute surface proteins from NeutrAvidin beads, samples were denatured for 5 min at 95°C with BME and separated on 4–12% SDS gels. Molecular weight standards (kDa) are indicated on the left . c Cell lysates (20 μg each lane) of CHO-K1 cells stably overexpressing APP ER (KKAA), were incubated with SDS sample loading buffer (+ BME) and heat denatured for 10 min at the indicated temperatures (4–85°C). APP monomers and SDS stable dimers were detected, using the monoclonal anti myc antibody (9E10), shown on one representative Western blot. d APP dimers and monomers were quantified by densitometric analysis of Western blots, as the one shown in c . In each case, intensities at 4°C were set as 100%. Diagram shows relative intensity (%) of APP monomers and dimers, plotted against different temperatures. Data are ( n ≥ 3) ± SEM, one-way ANOVA
    Gibco 2 Mercaptoethanol also known as beta mercaptoethanol or BME is a potent reducing agent used in cell culture media to prevent toxic levels of oxygen radicals 2 Mercaptoethanol is not stable in solution so most protocols require daily supplementation Gibco 2 Mercaptoethanol contains 2 mercaptoethanol at a concentration of 55 mM in Dulbecco s phosphate buffered saline DPBS cGMP manufacturing and quality systemGibco Reducing Agent is manufactured at a cGMP compliant facility located in Grand Island New York The facility is registered with the FDA as a medical device manufacturer and is certified to ISO 13485 standards
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    Images

    1) Product Images from "APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms"

    Article Title: APP dimer formation is initiated in the endoplasmic reticulum and differs between APP isoforms

    Journal: Cellular and Molecular Life Sciences

    doi: 10.1007/s00018-011-0882-4

    ER-retention of APP by addition of the di-lysine motif KKAA induces SDS stable homo-dimers in an oxidizing cellular surrounding. a Schematic illustration of the APP domain structure and the used dilysine retention constructs. APP isoform 695 (APP695) was fused to a C-terminal myc-tag, followed by either a KKAA ER retention motif, or a “leaky” KKFF motif allowing trafficking to the cis -Golgi compartment. The E1 domain, acidic domain, E2 domain, transmembrane domain (TM), and the intracellular domain are indicated. b CHO-K1 cells stably over expressing the respective APP695 wt or APP695 retention constructs were subjected to cell surface biotinylation. To inhibit endocytosis from the cell surface, AP180 D/N (lane four) was transiently co-expressed. At 24-h post-transfection, cell surface proteins were labeled with sulfo NHS-SS-biotin at 4°C, prior to lysis. Biotinylated samples were precipitated with NeutrAvidin agarose beads and analyzed by SDS-PAGE and Western blot (PD: NeutrAvidin; right panel ). As input controls, 20 μg of cell lysates were used (input; left panel ). APP full length, CTFs and AP180 D/N were probed with 9E10 antibody. Monoclonal α-Tubulin antibody served as a loading control to verify the absence of endomembrane contaminants in the biotinylation. For the input control, all samples were treated with SDS sample loading buffer, containing β-mercaptoethanol (BME) without heat denaturing prior to SDS gel electrophoresis. To elute surface proteins from NeutrAvidin beads, samples were denatured for 5 min at 95°C with BME and separated on 4–12% SDS gels. Molecular weight standards (kDa) are indicated on the left . c Cell lysates (20 μg each lane) of CHO-K1 cells stably overexpressing APP ER (KKAA), were incubated with SDS sample loading buffer (+ BME) and heat denatured for 10 min at the indicated temperatures (4–85°C). APP monomers and SDS stable dimers were detected, using the monoclonal anti myc antibody (9E10), shown on one representative Western blot. d APP dimers and monomers were quantified by densitometric analysis of Western blots, as the one shown in c . In each case, intensities at 4°C were set as 100%. Diagram shows relative intensity (%) of APP monomers and dimers, plotted against different temperatures. Data are ( n ≥ 3) ± SEM, one-way ANOVA
    Figure Legend Snippet: ER-retention of APP by addition of the di-lysine motif KKAA induces SDS stable homo-dimers in an oxidizing cellular surrounding. a Schematic illustration of the APP domain structure and the used dilysine retention constructs. APP isoform 695 (APP695) was fused to a C-terminal myc-tag, followed by either a KKAA ER retention motif, or a “leaky” KKFF motif allowing trafficking to the cis -Golgi compartment. The E1 domain, acidic domain, E2 domain, transmembrane domain (TM), and the intracellular domain are indicated. b CHO-K1 cells stably over expressing the respective APP695 wt or APP695 retention constructs were subjected to cell surface biotinylation. To inhibit endocytosis from the cell surface, AP180 D/N (lane four) was transiently co-expressed. At 24-h post-transfection, cell surface proteins were labeled with sulfo NHS-SS-biotin at 4°C, prior to lysis. Biotinylated samples were precipitated with NeutrAvidin agarose beads and analyzed by SDS-PAGE and Western blot (PD: NeutrAvidin; right panel ). As input controls, 20 μg of cell lysates were used (input; left panel ). APP full length, CTFs and AP180 D/N were probed with 9E10 antibody. Monoclonal α-Tubulin antibody served as a loading control to verify the absence of endomembrane contaminants in the biotinylation. For the input control, all samples were treated with SDS sample loading buffer, containing β-mercaptoethanol (BME) without heat denaturing prior to SDS gel electrophoresis. To elute surface proteins from NeutrAvidin beads, samples were denatured for 5 min at 95°C with BME and separated on 4–12% SDS gels. Molecular weight standards (kDa) are indicated on the left . c Cell lysates (20 μg each lane) of CHO-K1 cells stably overexpressing APP ER (KKAA), were incubated with SDS sample loading buffer (+ BME) and heat denatured for 10 min at the indicated temperatures (4–85°C). APP monomers and SDS stable dimers were detected, using the monoclonal anti myc antibody (9E10), shown on one representative Western blot. d APP dimers and monomers were quantified by densitometric analysis of Western blots, as the one shown in c . In each case, intensities at 4°C were set as 100%. Diagram shows relative intensity (%) of APP monomers and dimers, plotted against different temperatures. Data are ( n ≥ 3) ± SEM, one-way ANOVA

    Techniques Used: Construct, Stable Transfection, Expressing, Transfection, Labeling, Lysis, SDS Page, Western Blot, SDS-Gel, Electrophoresis, Molecular Weight, Incubation

    APP wt homodimers are formed in the ER but also occur at the cell surface. a N2a cells were transiently co-transfected with NT HA APP695 CT Split GFP 1–10 and NT HA APP695 CT Split GFP 11. The cells were fixed with paraformaldehyde and immunostained with ER marker Grp78, followed by incubation with AlexaFlour-594 conjugated secondary antibody. The green fluorescence represents the APP dimer, induced by bimolecular fluorescence complementation (BiFC). Co-staining with Grp78 revealed colocalization of the APP dimer ( inset ) with the ER. b Single transfections of N2a cells with either NT HA APP695 CT Split GFP 1–10 or NT HA APP695 CT Split GFP 11. APP expression was verified with HA antibody, confirming a non-perturbed distribution ( right panel , red ). The green channel does not show any specific fluorescence. Scale bar is 10 μm. c N2a cells were transiently transfected with NT HA APP695 CT Split GFP 1–10, NT HA APP695 CT Split GFP 11 or GFP only. Cell lysates were analyzed via Western blotting for APP full length ( top part ), APP CTFs ( middle part ) and GFP, or GFP-containing CTFs ( bottom part ). Note that GFP antibody does not recognize GFP 11 alone. d CHO-K1 cells stably overexpressing APP 695 wt were pretreated for 1 h at 37°C in the presence of 10 μg/ml brefeldin A (BFA), or DMSO (vehicle) for 1 h to block protein secretion from the ER. Subsequently, cells were either directly lysed (BFA), or medium containing BFA was removed, and cells were incubated for additional 30 min at 37°C with 10 μM chlorpromazine (BFA/CPZ), to allow transport to the cell surface, but inhibit further endocytosis. Lysates were analyzed either under non-reducing (+β mercaptoethanol; −95°C), or reducing conditions (+β-mercaptoethanol; +95°C). Note that cells pretreated with BFA, followed by chlorpromazine exposure (BFA/CPZ), display two upper SDS-resistant bands migrating with a slight size shift, indicating different glycosylation patterns (dimer i/m). Note that strong denaturing conditions (+95°C) result in the disappearance of the upper migrating bands, suggesting disulfide bond formation. The separating line indicates different exposure times to visualize dimer formation in treated cells, whereas APP ER overexpressing cells served as size reference for dimers. e Cells were treated as described under d , and subjected to cell surface biotinylation to confirm drug treatments. APP ER is completely absent from the surface, whereas only minor quantities of mature APP reach the surface upon BFA treatment. Removal of BFA, and subsequent incubation with chlorpromazine (BFA/CPZ), strongly increases surface exposed mature APP, compared to vehicle control. Note that no dimers are recovered in biotinylation, because NeutrAvidin beads were boiled in BME containing sample buffer, to release biotin conjugated proteins
    Figure Legend Snippet: APP wt homodimers are formed in the ER but also occur at the cell surface. a N2a cells were transiently co-transfected with NT HA APP695 CT Split GFP 1–10 and NT HA APP695 CT Split GFP 11. The cells were fixed with paraformaldehyde and immunostained with ER marker Grp78, followed by incubation with AlexaFlour-594 conjugated secondary antibody. The green fluorescence represents the APP dimer, induced by bimolecular fluorescence complementation (BiFC). Co-staining with Grp78 revealed colocalization of the APP dimer ( inset ) with the ER. b Single transfections of N2a cells with either NT HA APP695 CT Split GFP 1–10 or NT HA APP695 CT Split GFP 11. APP expression was verified with HA antibody, confirming a non-perturbed distribution ( right panel , red ). The green channel does not show any specific fluorescence. Scale bar is 10 μm. c N2a cells were transiently transfected with NT HA APP695 CT Split GFP 1–10, NT HA APP695 CT Split GFP 11 or GFP only. Cell lysates were analyzed via Western blotting for APP full length ( top part ), APP CTFs ( middle part ) and GFP, or GFP-containing CTFs ( bottom part ). Note that GFP antibody does not recognize GFP 11 alone. d CHO-K1 cells stably overexpressing APP 695 wt were pretreated for 1 h at 37°C in the presence of 10 μg/ml brefeldin A (BFA), or DMSO (vehicle) for 1 h to block protein secretion from the ER. Subsequently, cells were either directly lysed (BFA), or medium containing BFA was removed, and cells were incubated for additional 30 min at 37°C with 10 μM chlorpromazine (BFA/CPZ), to allow transport to the cell surface, but inhibit further endocytosis. Lysates were analyzed either under non-reducing (+β mercaptoethanol; −95°C), or reducing conditions (+β-mercaptoethanol; +95°C). Note that cells pretreated with BFA, followed by chlorpromazine exposure (BFA/CPZ), display two upper SDS-resistant bands migrating with a slight size shift, indicating different glycosylation patterns (dimer i/m). Note that strong denaturing conditions (+95°C) result in the disappearance of the upper migrating bands, suggesting disulfide bond formation. The separating line indicates different exposure times to visualize dimer formation in treated cells, whereas APP ER overexpressing cells served as size reference for dimers. e Cells were treated as described under d , and subjected to cell surface biotinylation to confirm drug treatments. APP ER is completely absent from the surface, whereas only minor quantities of mature APP reach the surface upon BFA treatment. Removal of BFA, and subsequent incubation with chlorpromazine (BFA/CPZ), strongly increases surface exposed mature APP, compared to vehicle control. Note that no dimers are recovered in biotinylation, because NeutrAvidin beads were boiled in BME containing sample buffer, to release biotin conjugated proteins

    Techniques Used: Transfection, Marker, Incubation, Fluorescence, Bimolecular Fluorescence Complementation Assay, Staining, Expressing, Western Blot, Stable Transfection, Blocking Assay

    2) Product Images from "Access to a main alphaherpesvirus receptor, located basolaterally in the respiratory epithelium, is masked by intercellular junctions"

    Article Title: Access to a main alphaherpesvirus receptor, located basolaterally in the respiratory epithelium, is masked by intercellular junctions

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-16804-5

    Disruption of ICJ in respiratory mucosal explants. ( a ) The percentage of intercellular spaces in equine respiratory mucosal explants after 1 h treatment with PBS (control), DTT, β-mercaptoethanol, NAC or EGTA (left) and 24 h after the 1 h treatment (right). Three independent experiments were performed and data are represented as means + SD, different lower case letters indicate significant (P
    Figure Legend Snippet: Disruption of ICJ in respiratory mucosal explants. ( a ) The percentage of intercellular spaces in equine respiratory mucosal explants after 1 h treatment with PBS (control), DTT, β-mercaptoethanol, NAC or EGTA (left) and 24 h after the 1 h treatment (right). Three independent experiments were performed and data are represented as means + SD, different lower case letters indicate significant (P

    Techniques Used:

    3) Product Images from "Binding of Recombinant Feline Immunodeficiency Virus Surface Glycoprotein to Feline Cells: Role of CXCR4, Cell-Surface Heparans, and an Unidentified Non-CXCR4 Receptor"

    Article Title: Binding of Recombinant Feline Immunodeficiency Virus Surface Glycoprotein to Feline Cells: Role of CXCR4, Cell-Surface Heparans, and an Unidentified Non-CXCR4 Receptor

    Journal: Journal of Virology

    doi: 10.1128/JVI.75.10.4528-4539.2001

    Construction of an FIV SU-immunoadhesin. (A) The FIV genome is represented at the top. The FIV Env region contains a leader (L) sequence followed by the surface (gp95) and transmembrane (gp36) subunits. FIV gp95, including the leader sequence, was cloned in frame to the hinge (H) region of human IgG Fc. The recombinant immunoadhesin proteins were stably transfected in CHO cells and batch purified from cell supernatants by affinity chromatography over protein A. (B) Samples (500 ng) of PPR (lanes PP) or 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE in the presence or absence of β-mercaptoethanol (β-ME) and stained by Coomassie blue. (C) Samples of PPR (lanes PP) and 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE under reducing conditions and immunoblotted with an antibody specific for human IgG1 Fc (α-Fc) or FIV Env (α-Env).
    Figure Legend Snippet: Construction of an FIV SU-immunoadhesin. (A) The FIV genome is represented at the top. The FIV Env region contains a leader (L) sequence followed by the surface (gp95) and transmembrane (gp36) subunits. FIV gp95, including the leader sequence, was cloned in frame to the hinge (H) region of human IgG Fc. The recombinant immunoadhesin proteins were stably transfected in CHO cells and batch purified from cell supernatants by affinity chromatography over protein A. (B) Samples (500 ng) of PPR (lanes PP) or 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE in the presence or absence of β-mercaptoethanol (β-ME) and stained by Coomassie blue. (C) Samples of PPR (lanes PP) and 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE under reducing conditions and immunoblotted with an antibody specific for human IgG1 Fc (α-Fc) or FIV Env (α-Env).

    Techniques Used: Sequencing, Clone Assay, Recombinant, Stable Transfection, Transfection, Purification, Affinity Chromatography, SDS Page, Staining

    4) Product Images from "Structural features and oligomeric nature of human podocin domain"

    Article Title: Structural features and oligomeric nature of human podocin domain

    Journal: Biochemistry and Biophysics Reports

    doi: 10.1016/j.bbrep.2020.100774

    Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.
    Figure Legend Snippet: Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.

    Techniques Used: Fluorescence

    5) Product Images from "Structural features and oligomeric nature of human podocin domain"

    Article Title: Structural features and oligomeric nature of human podocin domain

    Journal: Biochemistry and Biophysics Reports

    doi: 10.1016/j.bbrep.2020.100774

    Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.
    Figure Legend Snippet: Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.

    Techniques Used: Fluorescence

    6) Product Images from "ER Proteostasis Regulators Reduce Amyloidogenic Light Chain Secretion Through an On-Target, ATF6-Independent Mechanism"

    Article Title: ER Proteostasis Regulators Reduce Amyloidogenic Light Chain Secretion Through an On-Target, ATF6-Independent Mechanism

    Journal: bioRxiv

    doi: 10.1101/2020.05.15.098145

    Compound 147 reduces ALLC secretion through a mechanism involving compound metabolic activation and covalent protein modification. A. Illustration showing the metabolic activation of 147 to a quinone imide ( 147-QI ) and quinone methide ( 147 - QM ). These reactive electrophiles covalently modify ER proteins including multiple PDIs. The ‘A’-ring, linker, and ‘B’-ring of 147 are indicated. Specific steps inhibited by resveratrol and β-mercaptoethanol (BME) are also indicated. Adapted from ( Paxman et al., 2018 ). B. Graph showing normalized amounts of ALLC in conditioned media from ALMC-2 cells treated for 18 hr with vehicle, 147 (10 μM) or the indicated 147 ‘A’-ring analog (10 μM). ALLC was quantified by ELISA. Error bars show SEM for n=10 replicates across two independent experiments. ***p
    Figure Legend Snippet: Compound 147 reduces ALLC secretion through a mechanism involving compound metabolic activation and covalent protein modification. A. Illustration showing the metabolic activation of 147 to a quinone imide ( 147-QI ) and quinone methide ( 147 - QM ). These reactive electrophiles covalently modify ER proteins including multiple PDIs. The ‘A’-ring, linker, and ‘B’-ring of 147 are indicated. Specific steps inhibited by resveratrol and β-mercaptoethanol (BME) are also indicated. Adapted from ( Paxman et al., 2018 ). B. Graph showing normalized amounts of ALLC in conditioned media from ALMC-2 cells treated for 18 hr with vehicle, 147 (10 μM) or the indicated 147 ‘A’-ring analog (10 μM). ALLC was quantified by ELISA. Error bars show SEM for n=10 replicates across two independent experiments. ***p

    Techniques Used: Activation Assay, Modification, Enzyme-linked Immunosorbent Assay

    7) Product Images from "The NS1 Protein of Influenza A Virus Participates in Necroptosis by Interacting with MLKL and Increasing Its Oligomerization and Membrane Translocation"

    Article Title: The NS1 Protein of Influenza A Virus Participates in Necroptosis by Interacting with MLKL and Increasing Its Oligomerization and Membrane Translocation

    Journal: Journal of Virology

    doi: 10.1128/JVI.01835-18

    NS1 enhances MLKL oligomerization and membrane translocation. (A) HEK293T cells were cotransfected with the Flag-tagged MLKL-expressing plasmid and increasing amounts of the NS1-expressing plasmid. At 36 h posttransfection, cell lysates were separated into the total, cytoplasmic (C), or membrane (M) fraction. The cell lysates were resolved on SDS-PAGE gels with (reducing) or without (nonreducing) β-mercaptoethanol and analyzed by Western blotting using the indicated antibodies. (B) HEK293T cells were cotransfected with the Flag-tagged MLKL-expressing plasmid and either the WT NS1- or NS1(R38A/K41A)-expressing plasmid. At 36 h posttransfection, cell lysates were harvested and subjected to assays as described above for panel A. (C) Differentiated THP1 cells were either mock infected or infected with PR8 virus at an MOI of 10. At 8 h p.i., cell lysates were harvested and subjected to assays as described above for panel A.
    Figure Legend Snippet: NS1 enhances MLKL oligomerization and membrane translocation. (A) HEK293T cells were cotransfected with the Flag-tagged MLKL-expressing plasmid and increasing amounts of the NS1-expressing plasmid. At 36 h posttransfection, cell lysates were separated into the total, cytoplasmic (C), or membrane (M) fraction. The cell lysates were resolved on SDS-PAGE gels with (reducing) or without (nonreducing) β-mercaptoethanol and analyzed by Western blotting using the indicated antibodies. (B) HEK293T cells were cotransfected with the Flag-tagged MLKL-expressing plasmid and either the WT NS1- or NS1(R38A/K41A)-expressing plasmid. At 36 h posttransfection, cell lysates were harvested and subjected to assays as described above for panel A. (C) Differentiated THP1 cells were either mock infected or infected with PR8 virus at an MOI of 10. At 8 h p.i., cell lysates were harvested and subjected to assays as described above for panel A.

    Techniques Used: Translocation Assay, Expressing, Plasmid Preparation, SDS Page, Western Blot, Infection

    8) Product Images from "Uncyclized xanthommatin is a key ommochrome intermediate in invertebrate coloration"

    Article Title: Uncyclized xanthommatin is a key ommochrome intermediate in invertebrate coloration

    Journal: bioRxiv

    doi: 10.1101/666529

    Ommatins are altered by addition of β-mercaptoethanol. Ommatins were separated by liquid chromatography and analysed by absorption, mass and tandem mass spectroscopies. ( A ) Chromatograms of acidified methanol (MeOH-HCl) extract of purified ommochromasomes and synthesized xanthommatin solubilized in phosphate buffer with β-mercaptoethanol. Only the signals of the multiple reaction monitoring (MRM) for the 456- and 500 m/z -associated compounds are shown. ( B-D ) Analytical characterization of the 456- and the 500- m/z -associated compounds present in phosphate buffer with β-mercaptoethanol. (B) Absorbance spectra. Wavelengths of peaks are reported. (C) Mass spectra in positive mode. Monocharged and double-charged ions are indicated in black and blue fonts, respectively. Mass losses of in-source fragments are indicated in parenthesis. (D) Tandem mass spectra in positive mode of the molecular ions [M+H] + . Main fragments are indicated in black fonts. Losses corresponding to the typical fragmentation of the amino acid chain of ommatins are reported in green. ( E ) Kinetics of formation of the 456- and 500- m/z -associated compounds in phosphate buffer with β-mercaptoethanol at 20 °C in darkness. The two compounds were monitored and quantified by MRM. Values are mean ± S.D. of four samples. See File S2 for information on regression analyses.
    Figure Legend Snippet: Ommatins are altered by addition of β-mercaptoethanol. Ommatins were separated by liquid chromatography and analysed by absorption, mass and tandem mass spectroscopies. ( A ) Chromatograms of acidified methanol (MeOH-HCl) extract of purified ommochromasomes and synthesized xanthommatin solubilized in phosphate buffer with β-mercaptoethanol. Only the signals of the multiple reaction monitoring (MRM) for the 456- and 500 m/z -associated compounds are shown. ( B-D ) Analytical characterization of the 456- and the 500- m/z -associated compounds present in phosphate buffer with β-mercaptoethanol. (B) Absorbance spectra. Wavelengths of peaks are reported. (C) Mass spectra in positive mode. Monocharged and double-charged ions are indicated in black and blue fonts, respectively. Mass losses of in-source fragments are indicated in parenthesis. (D) Tandem mass spectra in positive mode of the molecular ions [M+H] + . Main fragments are indicated in black fonts. Losses corresponding to the typical fragmentation of the amino acid chain of ommatins are reported in green. ( E ) Kinetics of formation of the 456- and 500- m/z -associated compounds in phosphate buffer with β-mercaptoethanol at 20 °C in darkness. The two compounds were monitored and quantified by MRM. Values are mean ± S.D. of four samples. See File S2 for information on regression analyses.

    Techniques Used: Liquid Chromatography, Purification, Synthesized

    9) Product Images from "Characterization and Use of Mammalian-Expressed Vaccinia Virus Extracellular Membrane Proteins for Quantification of the Humoral Immune Response to Smallpox Vaccines ▿"

    Article Title: Characterization and Use of Mammalian-Expressed Vaccinia Virus Extracellular Membrane Proteins for Quantification of the Humoral Immune Response to Smallpox Vaccines ▿

    Journal: Clinical and Vaccine Immunology : CVI

    doi: 10.1128/CVI.00050-07

    Analysis of immune serum from mice immunized with an HA deletion mutant vaccinia virus strain and noninfectious MV particles. (A) Hyperimmune antiserum anti-vA5Lint was obtained from BALB/c mice inoculated i.p. with a recombinant WR-strain vaccinia virus that lacks the A56R (HA) gene, vA5Lint, using a prime-boost schedule. (B) Hyperimmune antiserum anti-MV was obtained from mice inoculated s.c. with noninfectious WR strain vaccinia virus MV particles (4.0 × 10 7 PFU equivalents) using a prime-boost schedule. A33R, A34R, A56R, and B5R protein preparations were treated with (+) and without (−) β-mercaptoethanol (β-ME) prior to SDS-PAGE and protein transfer onto PVDF membranes. The PVDF membranes were incubated with mouse immune sera, followed by a second incubation with an anti-mouse IgG antibody conjugated to HRP. Protein bands were detected by chemiluminescence. Masses of protein markers are indicated on the left.
    Figure Legend Snippet: Analysis of immune serum from mice immunized with an HA deletion mutant vaccinia virus strain and noninfectious MV particles. (A) Hyperimmune antiserum anti-vA5Lint was obtained from BALB/c mice inoculated i.p. with a recombinant WR-strain vaccinia virus that lacks the A56R (HA) gene, vA5Lint, using a prime-boost schedule. (B) Hyperimmune antiserum anti-MV was obtained from mice inoculated s.c. with noninfectious WR strain vaccinia virus MV particles (4.0 × 10 7 PFU equivalents) using a prime-boost schedule. A33R, A34R, A56R, and B5R protein preparations were treated with (+) and without (−) β-mercaptoethanol (β-ME) prior to SDS-PAGE and protein transfer onto PVDF membranes. The PVDF membranes were incubated with mouse immune sera, followed by a second incubation with an anti-mouse IgG antibody conjugated to HRP. Protein bands were detected by chemiluminescence. Masses of protein markers are indicated on the left.

    Techniques Used: Mouse Assay, Mutagenesis, Recombinant, SDS Page, Incubation

    10) Product Images from "Rotavirus variant replicates efficiently although encoding an aberrant NSP3 that fails to induce nuclear localization of poly(A)-binding protein"

    Article Title: Rotavirus variant replicates efficiently although encoding an aberrant NSP3 that fails to induce nuclear localization of poly(A)-binding protein

    Journal: The Journal of General Virology

    doi: 10.1099/vir.0.041830-0

    Dimerization of NSP3 and NSP3m. (a) 35 S-labelled proteins from mock-infected or SA11-4F- or SA11-4Fg7re-infected cells were incubated at 23 or 95 °C in sample buffer containing SDS and β-mercaptoethanol and detected by gel electrophoresis
    Figure Legend Snippet: Dimerization of NSP3 and NSP3m. (a) 35 S-labelled proteins from mock-infected or SA11-4F- or SA11-4Fg7re-infected cells were incubated at 23 or 95 °C in sample buffer containing SDS and β-mercaptoethanol and detected by gel electrophoresis

    Techniques Used: Infection, Incubation, Nucleic Acid Electrophoresis

    11) Product Images from "In Vitro and In Vivo Analysis of Indocyanine Green-Labeled Panitumumab for Optical Imaging—A Cautionary Tale"

    Article Title: In Vitro and In Vivo Analysis of Indocyanine Green-Labeled Panitumumab for Optical Imaging—A Cautionary Tale

    Journal: Bioconjugate Chemistry

    doi: 10.1021/bc500312w

    SDS-PAGE of (A) SE-HPLC-isolated ICG-sOSu-panitumumab conjugates and aggregates, and (B) reaction mixture, under nonreducing and reducing conditions with β-mercaptoethanol. Panitumumab served as a reference. Colloidal blue protein staining and optical imaging were performed: M, marker; 1, intact panitumumab antibody; 2, 1 ; 3, 2 ; 4, 3 ; 5, ICG-sOSu aggregates (from 20× reaction, peak with RT = 12.5 min); 6, ICG-sOSu aggregates (from 20× reaction, peak with RT = 14.5 min); 7, ICG-sOSu-panitumumab reaction mixture (10×, without purification); 8, ICG-sOSu alone incubated in conjugation buffer for 1 h at 37 °C as a control. White arrow: heavy chain; yellow arrow: light chain; blue arrow: free dye.
    Figure Legend Snippet: SDS-PAGE of (A) SE-HPLC-isolated ICG-sOSu-panitumumab conjugates and aggregates, and (B) reaction mixture, under nonreducing and reducing conditions with β-mercaptoethanol. Panitumumab served as a reference. Colloidal blue protein staining and optical imaging were performed: M, marker; 1, intact panitumumab antibody; 2, 1 ; 3, 2 ; 4, 3 ; 5, ICG-sOSu aggregates (from 20× reaction, peak with RT = 12.5 min); 6, ICG-sOSu aggregates (from 20× reaction, peak with RT = 14.5 min); 7, ICG-sOSu-panitumumab reaction mixture (10×, without purification); 8, ICG-sOSu alone incubated in conjugation buffer for 1 h at 37 °C as a control. White arrow: heavy chain; yellow arrow: light chain; blue arrow: free dye.

    Techniques Used: SDS Page, High Performance Liquid Chromatography, Isolation, Staining, Optical Imaging, Marker, Purification, Incubation, Conjugation Assay

    12) Product Images from "Binding of Recombinant Feline Immunodeficiency Virus Surface Glycoprotein to Feline Cells: Role of CXCR4, Cell-Surface Heparans, and an Unidentified Non-CXCR4 Receptor"

    Article Title: Binding of Recombinant Feline Immunodeficiency Virus Surface Glycoprotein to Feline Cells: Role of CXCR4, Cell-Surface Heparans, and an Unidentified Non-CXCR4 Receptor

    Journal: Journal of Virology

    doi: 10.1128/JVI.75.10.4528-4539.2001

    Construction of an FIV SU-immunoadhesin. (A) The FIV genome is represented at the top. The FIV Env region contains a leader (L) sequence followed by the surface (gp95) and transmembrane (gp36) subunits. FIV gp95, including the leader sequence, was cloned in frame to the hinge (H) region of human IgG Fc. The recombinant immunoadhesin proteins were stably transfected in CHO cells and batch purified from cell supernatants by affinity chromatography over protein A. (B) Samples (500 ng) of PPR (lanes PP) or 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE in the presence or absence of β-mercaptoethanol (β-ME) and stained by Coomassie blue. (C) Samples of PPR (lanes PP) and 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE under reducing conditions and immunoblotted with an antibody specific for human IgG1 Fc (α-Fc) or FIV Env (α-Env).
    Figure Legend Snippet: Construction of an FIV SU-immunoadhesin. (A) The FIV genome is represented at the top. The FIV Env region contains a leader (L) sequence followed by the surface (gp95) and transmembrane (gp36) subunits. FIV gp95, including the leader sequence, was cloned in frame to the hinge (H) region of human IgG Fc. The recombinant immunoadhesin proteins were stably transfected in CHO cells and batch purified from cell supernatants by affinity chromatography over protein A. (B) Samples (500 ng) of PPR (lanes PP) or 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE in the presence or absence of β-mercaptoethanol (β-ME) and stained by Coomassie blue. (C) Samples of PPR (lanes PP) and 34TF10 (lanes 34) gp95-Fc were subjected to SDS-PAGE under reducing conditions and immunoblotted with an antibody specific for human IgG1 Fc (α-Fc) or FIV Env (α-Env).

    Techniques Used: Sequencing, Clone Assay, Recombinant, Stable Transfection, Transfection, Purification, Affinity Chromatography, SDS Page, Staining

    13) Product Images from "Rotavirus variant replicates efficiently although encoding an aberrant NSP3 that fails to induce nuclear localization of poly(A)-binding protein"

    Article Title: Rotavirus variant replicates efficiently although encoding an aberrant NSP3 that fails to induce nuclear localization of poly(A)-binding protein

    Journal: The Journal of General Virology

    doi: 10.1099/vir.0.041830-0

    Dimerization of NSP3 and NSP3m. (a) 35 S-labelled proteins from mock-infected or SA11-4F- or SA11-4Fg7re-infected cells were incubated at 23 or 95 °C in sample buffer containing SDS and β-mercaptoethanol and detected by gel electrophoresis
    Figure Legend Snippet: Dimerization of NSP3 and NSP3m. (a) 35 S-labelled proteins from mock-infected or SA11-4F- or SA11-4Fg7re-infected cells were incubated at 23 or 95 °C in sample buffer containing SDS and β-mercaptoethanol and detected by gel electrophoresis

    Techniques Used: Infection, Incubation, Nucleic Acid Electrophoresis

    14) Product Images from "A constitutively monomeric UVR8 photoreceptor allele confers enhanced UV-B photomorphogenesis"

    Article Title: A constitutively monomeric UVR8 photoreceptor allele confers enhanced UV-B photomorphogenesis

    Journal: bioRxiv

    doi: 10.1101/2020.08.02.233007

    Characterization of UVR8 G101S,W285A lines. a Dimer/monomer status of UVR8 from DSP-crosslinked extracts of various UVR8-overexpressing lines under a 35S or XVE-responsive promoter. UVR8 W285A - and XVE:UVR8 G101S,W285A -expressing lines were grown on 5 μM estradiol. Crosslinking was reversed by addition of 5% β-mercaptoethanol. UGPase is shown as loading control. b Representative images and quantification of hypocotyl length of seedlings of wild type (Ws), uvr8-7 , uvr8-7 /Pro 35S :UVR8 W285A (W285A-OX), and three independent lines each of uvr8-7 /Pro UVR8 :UVR8 W285A (#9, #21, and #23) and uvr8-7 /Pro UVR8 :UVR8 G101S,W285A (#1, #2, and #4) grown in darkness ( N > 60). Shared letters indicate no statistically significant difference in the means ( P
    Figure Legend Snippet: Characterization of UVR8 G101S,W285A lines. a Dimer/monomer status of UVR8 from DSP-crosslinked extracts of various UVR8-overexpressing lines under a 35S or XVE-responsive promoter. UVR8 W285A - and XVE:UVR8 G101S,W285A -expressing lines were grown on 5 μM estradiol. Crosslinking was reversed by addition of 5% β-mercaptoethanol. UGPase is shown as loading control. b Representative images and quantification of hypocotyl length of seedlings of wild type (Ws), uvr8-7 , uvr8-7 /Pro 35S :UVR8 W285A (W285A-OX), and three independent lines each of uvr8-7 /Pro UVR8 :UVR8 W285A (#9, #21, and #23) and uvr8-7 /Pro UVR8 :UVR8 G101S,W285A (#1, #2, and #4) grown in darkness ( N > 60). Shared letters indicate no statistically significant difference in the means ( P

    Techniques Used: Expressing

    15) Product Images from "SMOC can act as both an antagonist and an expander of BMP signaling"

    Article Title: SMOC can act as both an antagonist and an expander of BMP signaling

    Journal: eLife

    doi: 10.7554/eLife.17935

    Dimeric X SMOC-1 is not dissociated by chelation or reduction. ( A ) SEC profile showing that X SMOC-1, refolded in the presence of 2 mM CaCl 2 , continues to migrate as a dimer (↓) upon the subsequent chelation of calcium ions by dialysis in the presence of 10.5 mM EDTA. ( B ) SDS-PAGE analysis of X SMOC-1, X SMOC-1 ∆EC, and X SMOC-1 EC in the presence (+) and absence (−) of β-mercaptoethanol shows that the X SMOC-1, X SMOC-1 ∆EC dimers are not linked by disulfide bonds. DOI: http://dx.doi.org/10.7554/eLife.17935.007
    Figure Legend Snippet: Dimeric X SMOC-1 is not dissociated by chelation or reduction. ( A ) SEC profile showing that X SMOC-1, refolded in the presence of 2 mM CaCl 2 , continues to migrate as a dimer (↓) upon the subsequent chelation of calcium ions by dialysis in the presence of 10.5 mM EDTA. ( B ) SDS-PAGE analysis of X SMOC-1, X SMOC-1 ∆EC, and X SMOC-1 EC in the presence (+) and absence (−) of β-mercaptoethanol shows that the X SMOC-1, X SMOC-1 ∆EC dimers are not linked by disulfide bonds. DOI: http://dx.doi.org/10.7554/eLife.17935.007

    Techniques Used: Size-exclusion Chromatography, SDS Page

    16) Product Images from "Feline Immunodeficiency Virus OrfA Is Distinct from Other Lentivirus Transactivators"

    Article Title: Feline Immunodeficiency Virus OrfA Is Distinct from Other Lentivirus Transactivators

    Journal: Journal of Virology

    doi: 10.1128/JVI.76.19.9624-9634.2002

    Purification of OrfA. (A) Western blot (lane 1) and Coomassie blue-stained gel (lanes 2 and 3) of purified OrfA showing the presence of both the 9- and the 18-kDa forms (lane 1) and the membrane-purified 9-kDa (lane 2) and its dimeric form (lane 3) analyzed by SDS-10 to 20% PAGE. (B) Dissociation of the OrfA dimer in the presence of 0.5 M β-mercaptoethanol (lane 5) and with simultaneous boiling (lane 6) or neither of these treatments (lane 4), as detected by Western blot analysis with anti-OrfA antibody. Lanes 1 to 3 show identical treatments of the 9-kDa OrfA protein.
    Figure Legend Snippet: Purification of OrfA. (A) Western blot (lane 1) and Coomassie blue-stained gel (lanes 2 and 3) of purified OrfA showing the presence of both the 9- and the 18-kDa forms (lane 1) and the membrane-purified 9-kDa (lane 2) and its dimeric form (lane 3) analyzed by SDS-10 to 20% PAGE. (B) Dissociation of the OrfA dimer in the presence of 0.5 M β-mercaptoethanol (lane 5) and with simultaneous boiling (lane 6) or neither of these treatments (lane 4), as detected by Western blot analysis with anti-OrfA antibody. Lanes 1 to 3 show identical treatments of the 9-kDa OrfA protein.

    Techniques Used: Purification, Western Blot, Staining, Polyacrylamide Gel Electrophoresis

    17) Product Images from "Potential of Adipose-Derived Mesenchymal Stem Cells and Skeletal Muscle-Derived Satellite Cells for Somatic Cell Nuclear Transfer Mediated Transgenesis in Arbas Cashmere Goats"

    Article Title: Potential of Adipose-Derived Mesenchymal Stem Cells and Skeletal Muscle-Derived Satellite Cells for Somatic Cell Nuclear Transfer Mediated Transgenesis in Arbas Cashmere Goats

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0093583

    Neuronal differentiation of gADSCs, gADSCs–pDsRed2-1, gMDSCs and gMDSCs–pDsRed2-1. gADSCs, gADSCs–pDsRed2-1, gMDSCs and gMDSCs–pDsRed2-1 were altered morphologically by incubation in induction medium containing β-mercaptoethanol. The cytoplasm began to shrink, and after 2 h the cell bodies became conical, triangular or round in shape with multiple protrusions resembling axons, the ends of which were primary and secondary bifurcated dendrites. Immunohistochemistry showed that the cells were NSE (green) positive after 3 h. Uninduced control cells were morphologically unaltered and did not express NSE. gADSCs, goat adipose-derived mesenchymal stem cells; gMDSCs, goat muscle-derived satellite cells; NSE, neuron-specific enolase.
    Figure Legend Snippet: Neuronal differentiation of gADSCs, gADSCs–pDsRed2-1, gMDSCs and gMDSCs–pDsRed2-1. gADSCs, gADSCs–pDsRed2-1, gMDSCs and gMDSCs–pDsRed2-1 were altered morphologically by incubation in induction medium containing β-mercaptoethanol. The cytoplasm began to shrink, and after 2 h the cell bodies became conical, triangular or round in shape with multiple protrusions resembling axons, the ends of which were primary and secondary bifurcated dendrites. Immunohistochemistry showed that the cells were NSE (green) positive after 3 h. Uninduced control cells were morphologically unaltered and did not express NSE. gADSCs, goat adipose-derived mesenchymal stem cells; gMDSCs, goat muscle-derived satellite cells; NSE, neuron-specific enolase.

    Techniques Used: Incubation, Immunohistochemistry, Derivative Assay

    18) Product Images from "Characterization and Use of Mammalian-Expressed Vaccinia Virus Extracellular Membrane Proteins for Quantification of the Humoral Immune Response to Smallpox Vaccines ▿"

    Article Title: Characterization and Use of Mammalian-Expressed Vaccinia Virus Extracellular Membrane Proteins for Quantification of the Humoral Immune Response to Smallpox Vaccines ▿

    Journal: Clinical and Vaccine Immunology : CVI

    doi: 10.1128/CVI.00050-07

    Analysis of immune serum from mice immunized with an HA deletion mutant vaccinia virus strain and noninfectious MV particles. (A) Hyperimmune antiserum anti-vA5Lint was obtained from BALB/c mice inoculated i.p. with a recombinant WR-strain vaccinia virus that lacks the A56R (HA) gene, vA5Lint, using a prime-boost schedule. (B) Hyperimmune antiserum anti-MV was obtained from mice inoculated s.c. with noninfectious WR strain vaccinia virus MV particles (4.0 × 10 7 PFU equivalents) using a prime-boost schedule. A33R, A34R, A56R, and B5R protein preparations were treated with (+) and without (−) β-mercaptoethanol (β-ME) prior to SDS-PAGE and protein transfer onto PVDF membranes. The PVDF membranes were incubated with mouse immune sera, followed by a second incubation with an anti-mouse IgG antibody conjugated to HRP. Protein bands were detected by chemiluminescence. Masses of protein markers are indicated on the left.
    Figure Legend Snippet: Analysis of immune serum from mice immunized with an HA deletion mutant vaccinia virus strain and noninfectious MV particles. (A) Hyperimmune antiserum anti-vA5Lint was obtained from BALB/c mice inoculated i.p. with a recombinant WR-strain vaccinia virus that lacks the A56R (HA) gene, vA5Lint, using a prime-boost schedule. (B) Hyperimmune antiserum anti-MV was obtained from mice inoculated s.c. with noninfectious WR strain vaccinia virus MV particles (4.0 × 10 7 PFU equivalents) using a prime-boost schedule. A33R, A34R, A56R, and B5R protein preparations were treated with (+) and without (−) β-mercaptoethanol (β-ME) prior to SDS-PAGE and protein transfer onto PVDF membranes. The PVDF membranes were incubated with mouse immune sera, followed by a second incubation with an anti-mouse IgG antibody conjugated to HRP. Protein bands were detected by chemiluminescence. Masses of protein markers are indicated on the left.

    Techniques Used: Mouse Assay, Mutagenesis, Recombinant, SDS Page, Incubation

    19) Product Images from "Regulation of the epithelial Na+ channel by paraoxonase-2"

    Article Title: Regulation of the epithelial Na+ channel by paraoxonase-2

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M117.785253

    PON-2 co-immunoprecipitates with ENaC. Mouse PON-2 and mouse ENaC subunits were co-expressed in HEK293 cells as indicated. A C-terminal V5 epitope–tagged ENaC subunit (α, β, or γ) was expressed alone (single subunit) or with the other two untagged subunits to produce αβγ channels. Cell extracts were immunoprecipitated with anti-V5 antibodies. Both the immunoprecipitates ( IP ) ( left ) and total cell lysate ( right ) were subjected to SDS-PAGE and immunoblotting ( IB ) with either an anti-mouse PON-2 antibody ( top ) or the V5 antibody ( bottom ). The experiment was performed under non-reducing conditions (no β-mercaptoethanol in the sample buffer). The mobility of the Bio-Rad molecular weight standards ( MW ) is shown to the right of all blots. Three independent experiments were performed for each condition.
    Figure Legend Snippet: PON-2 co-immunoprecipitates with ENaC. Mouse PON-2 and mouse ENaC subunits were co-expressed in HEK293 cells as indicated. A C-terminal V5 epitope–tagged ENaC subunit (α, β, or γ) was expressed alone (single subunit) or with the other two untagged subunits to produce αβγ channels. Cell extracts were immunoprecipitated with anti-V5 antibodies. Both the immunoprecipitates ( IP ) ( left ) and total cell lysate ( right ) were subjected to SDS-PAGE and immunoblotting ( IB ) with either an anti-mouse PON-2 antibody ( top ) or the V5 antibody ( bottom ). The experiment was performed under non-reducing conditions (no β-mercaptoethanol in the sample buffer). The mobility of the Bio-Rad molecular weight standards ( MW ) is shown to the right of all blots. Three independent experiments were performed for each condition.

    Techniques Used: Immunoprecipitation, SDS Page, Molecular Weight

    Related Articles

    Modification:

    Article Title: Efficient Generation of Hepatoblasts From Human ES Cells and iPS Cells by Transient Overexpression of Homeobox Gene HEX
    Article Snippet: .. Human ESCs were maintained on a feeder layer of mitomycin-inactivated mouse embryonic fibroblasts (ICR; ReproCELL Incorporated, Tokyo, Japan) with Dulbecco's modified Eagle's medium/F-12 (Sigma, St Louis, MO) supplemented with 0.1 mmol/l 2-mercaptoethanol, 0.1 mmol/l nonessential amino acids, 2 mmol/l -glutamine, 20% GIBCO knockout serum replacement (Invitrogen), and 5 ng/ml bFGF (Sigma) in a humidified atmosphere of 3% CO2 and 97% air at 37 °C. .. Human ESCs were dissociated with 0.1 mg/ml dispase (Roche Diagnostics, Burgess Hill, UK) into small clumps, and subcultured every 5 or 6 days.

    Lysis:

    Article Title: Discovery and Characterization of the First Archaeal Dihydromethanopterin Reductase, an Iron-Sulfur Flavoprotein from Methanosarcina mazei
    Article Snippet: .. About 5 g of cells was suspended with 10 ml of lysis buffer A (50 mM sodium phosphate [pH 8.0], 300 mM sodium chloride, 15 mM 2-mercaptoethanol, 20 mM imidazole) and broken with a Thermo Scientific French press (Fisher Scientific) at 20,000 lb/in2 . .. The mixture was centrifuged with a Sorvall F18S rotor at 27,000 × g for 30 min at 4°C, and the supernatant was filtered with 0.45-μm syringe filters (Millipore, Billerica, MA).

    other:

    Article Title: Uncyclized xanthommatin is a key ommochrome intermediate in invertebrate coloration
    Article Snippet: Sucrose (99 %) and sulfurous acid (6 % SO2 ) were purchased from Alfa Aesar. β-Mercaptoethanol was purchased from BDH Chemicals.

    Knock-Out:

    Article Title: Efficient Generation of Hepatoblasts From Human ES Cells and iPS Cells by Transient Overexpression of Homeobox Gene HEX
    Article Snippet: .. Human ESCs were maintained on a feeder layer of mitomycin-inactivated mouse embryonic fibroblasts (ICR; ReproCELL Incorporated, Tokyo, Japan) with Dulbecco's modified Eagle's medium/F-12 (Sigma, St Louis, MO) supplemented with 0.1 mmol/l 2-mercaptoethanol, 0.1 mmol/l nonessential amino acids, 2 mmol/l -glutamine, 20% GIBCO knockout serum replacement (Invitrogen), and 5 ng/ml bFGF (Sigma) in a humidified atmosphere of 3% CO2 and 97% air at 37 °C. .. Human ESCs were dissociated with 0.1 mg/ml dispase (Roche Diagnostics, Burgess Hill, UK) into small clumps, and subcultured every 5 or 6 days.

    Ex Vivo:

    Article Title: EPO receptor circuits for primary erythroblast survival
    Article Snippet: .. Red cells then were lysed, and progenitors were collected through 50% FBS in PBS., For ex vivo expansions, cells were plated at 8 × 105 cells/mL (7 mL per 100-mm dish) in StemPro-34 (Invitrogen) supplemented with 2.5 U/mL EPO, 100 ng/mL mSCF, 1 μM dexamethasone, 1 μM beta-estradiol, 75 μg/mL h-transferrin, (Sigma-Aldrich, St Louis, MO), 0.5% BSA (StemCell Technologies, Vancouver, BC), 0.1 mM 2-mercaptoethanol, 100 U/mL penicillin G, 100 μg/mL streptomycin, 0.25 μg/mL amphotericin B (1XPSF) (Invitrogen), and 1.5 mM l -glutamine (ie, “SP34-EX” medium). .. In the isolation of Kitpos CD71high Ter119neg erythroblasts, Linpos cells first were depleted from ex vivo cultures using biotinylated antibodies to CD5 (Ly-1), CD45R/B220, CDllb (Mac1), Ter119, and Ly6G (Gr1; StemCell Technologies).

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    Thermo Fisher natamycin me β cd inclusion complex
    The selected appearance ( A ), decay ratio ( B ), and lesion diameter ( C ) of tomatoes from the control group, waxy corn starch-based coating (S coating) group, and <t>natamycin/ME-</t> β -CD incorporated waxy corn starch-based coating (N/ME- β -CD S coating) group after incubated with Botrytis cinerea at different storage times (days). The different lower-case letters at each time point indicate a significant difference at p
    Natamycin Me β Cd Inclusion Complex, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher β mercaptoethanol
    Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM <t>β-mercaptoethanol.</t> B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.
    β Mercaptoethanol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2456 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    The selected appearance ( A ), decay ratio ( B ), and lesion diameter ( C ) of tomatoes from the control group, waxy corn starch-based coating (S coating) group, and natamycin/ME- β -CD incorporated waxy corn starch-based coating (N/ME- β -CD S coating) group after incubated with Botrytis cinerea at different storage times (days). The different lower-case letters at each time point indicate a significant difference at p

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: The selected appearance ( A ), decay ratio ( B ), and lesion diameter ( C ) of tomatoes from the control group, waxy corn starch-based coating (S coating) group, and natamycin/ME- β -CD incorporated waxy corn starch-based coating (N/ME- β -CD S coating) group after incubated with Botrytis cinerea at different storage times (days). The different lower-case letters at each time point indicate a significant difference at p

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques: Incubation

    The selected appearance ( a ), weight loss ( b ), and color parameter a* value ( c ) of tomatoes from the control group, waxy corn starch-based coating (S coating) group, and natamycin/ME- β -CD incorporated waxy corn starch-based coating (N/ME- β -CD S coating) group at different storage times (days). The different lower-case letters at each time point indicate a significant difference at p

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: The selected appearance ( a ), weight loss ( b ), and color parameter a* value ( c ) of tomatoes from the control group, waxy corn starch-based coating (S coating) group, and natamycin/ME- β -CD incorporated waxy corn starch-based coating (N/ME- β -CD S coating) group at different storage times (days). The different lower-case letters at each time point indicate a significant difference at p

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques:

    The FTIR spectrum of (a) natamycin, (b) Methyl- β -Cyclodextrin (ME- β -CD), and (c) natamycin/ME- β -CD inclusion complex.

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: The FTIR spectrum of (a) natamycin, (b) Methyl- β -Cyclodextrin (ME- β -CD), and (c) natamycin/ME- β -CD inclusion complex.

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques:

    Phase solubility diagram of natamycin in the presence of Methyl- β -Cyclodextrin (ME- β -CD) at 293.2 K, 303.2 K, and 313.2 K.

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: Phase solubility diagram of natamycin in the presence of Methyl- β -Cyclodextrin (ME- β -CD) at 293.2 K, 303.2 K, and 313.2 K.

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques: Solubility

    The 1H NMR spectrum of natamycin/ME- β -CD inclusion complex ( a ) and natamycin ( b ) in DMSO-d6.

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: The 1H NMR spectrum of natamycin/ME- β -CD inclusion complex ( a ) and natamycin ( b ) in DMSO-d6.

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques: Nuclear Magnetic Resonance

    The proposed molecular inclusion mode of the natamycin/ME- β -CD inclusion complex.

    Journal: Molecules

    Article Title: Development of Starch-Based Antifungal Coatings by Incorporation of Natamycin/Methyl-β-Cyclodextrin Inclusion Complex for Postharvest Treatments on Cherry Tomato against Botrytis cinerea

    doi: 10.3390/molecules24213962

    Figure Lengend Snippet: The proposed molecular inclusion mode of the natamycin/ME- β -CD inclusion complex.

    Article Snippet: The fourier transform infrared spectroscopy (FTIR) measurements of natamycin, ME-β -CD, and natamycin/ME-β -CD inclusion complex were conducted using an FTIR Spectrometer (Nicolet iS5, Thermo Fisher, Waltham, MA, USA).

    Techniques:

    Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.

    Journal: Biochemistry and Biophysics Reports

    Article Title: Structural features and oligomeric nature of human podocin domain

    doi: 10.1016/j.bbrep.2020.100774

    Figure Lengend Snippet: Podocin domain exhibits secondary structural elements and tertiary packing : A. Far-UV CD spectrum of Podocin domain at 25 °C, pH 8 in 10mM potassium phosphate buffer supplemented with 150mM NaCl and 2mM β-mercaptoethanol. B. Near-UV CD spectrum representing the tertiary packing of the podocin domain. C. Fluorescence emission of the podocin domain recorded by exciting the protein at 287 nm.

    Article Snippet: The cells were harvested by centrifugation (13300×g , 20 min, and 4 °C) and sonicated in the opening buffer (50 mM potassium phosphate (pH 8.0), 0.3 M NaCl, 5 mM β-mercaptoethanol and 0.1% Triton X-100) followed by clarification by centrifugation at 18000×g for 45 min at 4 °C.

    Techniques: Fluorescence

    Compound 147 reduces ALLC secretion through a mechanism involving compound metabolic activation and covalent protein modification. A. Illustration showing the metabolic activation of 147 to a quinone imide ( 147-QI ) and quinone methide ( 147 - QM ). These reactive electrophiles covalently modify ER proteins including multiple PDIs. The ‘A’-ring, linker, and ‘B’-ring of 147 are indicated. Specific steps inhibited by resveratrol and β-mercaptoethanol (BME) are also indicated. Adapted from ( Paxman et al., 2018 ). B. Graph showing normalized amounts of ALLC in conditioned media from ALMC-2 cells treated for 18 hr with vehicle, 147 (10 μM) or the indicated 147 ‘A’-ring analog (10 μM). ALLC was quantified by ELISA. Error bars show SEM for n=10 replicates across two independent experiments. ***p

    Journal: bioRxiv

    Article Title: ER Proteostasis Regulators Reduce Amyloidogenic Light Chain Secretion Through an On-Target, ATF6-Independent Mechanism

    doi: 10.1101/2020.05.15.098145

    Figure Lengend Snippet: Compound 147 reduces ALLC secretion through a mechanism involving compound metabolic activation and covalent protein modification. A. Illustration showing the metabolic activation of 147 to a quinone imide ( 147-QI ) and quinone methide ( 147 - QM ). These reactive electrophiles covalently modify ER proteins including multiple PDIs. The ‘A’-ring, linker, and ‘B’-ring of 147 are indicated. Specific steps inhibited by resveratrol and β-mercaptoethanol (BME) are also indicated. Adapted from ( Paxman et al., 2018 ). B. Graph showing normalized amounts of ALLC in conditioned media from ALMC-2 cells treated for 18 hr with vehicle, 147 (10 μM) or the indicated 147 ‘A’-ring analog (10 μM). ALLC was quantified by ELISA. Error bars show SEM for n=10 replicates across two independent experiments. ***p

    Article Snippet: Cycloheximide (Fisher), resveratrol (SelleckChem), ISRIB (Sigma), MG132 (Selleckchem), chloroquine (Sigma), PF429242 (S1Pi; Tocris), β-mercaptoethanol (BME; Thermo Fisher), and bortezomib (MilliporeSigma) were all purchased commercially.

    Techniques: Activation Assay, Modification, Enzyme-linked Immunosorbent Assay