jbscreen classics 2  (Jena Bioscience)


Bioz Verified Symbol Jena Bioscience is a verified supplier
Bioz Manufacturer Symbol Jena Bioscience manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Name:
    JBScreen Classic 2
    Description:

    Catalog Number:
    CS-102L
    Price:
    149.0
    Category:
    Crystallography
    Size:
    24 solutions
    Buy from Supplier


    Structured Review

    Jena Bioscience jbscreen classics 2

    https://www.bioz.com/result/jbscreen classics 2/product/Jena Bioscience
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    jbscreen classics 2 - by Bioz Stars, 2021-06
    90/100 stars

    Images

    Related Articles

    Crystallization Assay:

    Article Title: Crystallization and preliminary crystallographic analysis of the transpeptidase domain of penicillin-binding protein 2B from Streptococcus pneumoniae
    Article Snippet: .. Crystallization conditions were screened by the sparse-matrix technique (Jancarik & Kim, 1991 ) using the components of Structure Screens 1 and 2 (Molecular Dimensions, Apopka, Florida, USA) and JBScreen Classics 2, 3, 5 and 6 (Jena Bioscience, Jena, Germany) kits supplemented with 10 m M DTT. .. All crystallization trials were set up manually and used sitting-drop vapour diffusion at 293 K. For each screen, 0.4 µl protein solution (4.7 mg ml−1 ) was mixed with an equal volume of reservoir solution and equilibrated against 100 µl reservoir solution.

    Article Title: Characterization of the binding of a glycosylated serine protease from Euphorbia cf. lactea latex to human fibrinogen.
    Article Snippet: In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC). .. In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC). .. In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC).

    Incubation:

    Article Title: Characterization of the binding of a glycosylated serine protease from Euphorbia cf. lactea latex to human fibrinogen.
    Article Snippet: In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC). .. In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC). .. In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by isothermal titration calorimetry (ITC).

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 90
    Jena Bioscience propargyl maleimide
    Optimisation of the Click-PEGylation technique. (A) Effect of protein concentration on labelling efficiency during the Click-PEG reaction. Coomassie-stained mobility shift gels of purified GAPDH under untreated conditions reacted by Click-PEG red , comparing starting concentrations of 1 and 0.1 mg protein/mL. Profile plots of the ‘+ catalyst’ lanes were performed in FIJI. (B) Effect of <t>propargyl-maleimide</t> concentration on Click-PEG labelling. Coomassie-stained mobility shift gels of purified GAPDH reacted by Click-PEG red comparing 5 and 50 mM propargyl-maleimide, under untreated, reduced (10 mM TCEP) and oxidised (1 mM diamide) conditions. * indicates a higher molecular weight band. (C) Quantification of GAPDH thiol redox state distribution from (B). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means ±range of n=2 independent experiments. (D) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Coomassie-stained gel of purified GAPDH under reduced conditions (10 mM TCEP) reacted by Click-PEG red , comparing incubation times of 10, 30 and 120 min. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (E) Quantification of GAPDH thiol redox state distribution from (D). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments. (F) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Time course as for (D), except that GAPDH redox state was assessed by Western blotting. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (G) Quantification of GAPDH thiol redox state distribution from (F). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments.
    Propargyl Maleimide, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/propargyl maleimide/product/Jena Bioscience
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    propargyl maleimide - by Bioz Stars, 2021-06
    90/100 stars
      Buy from Supplier

    85
    Jena Bioscience caged gtp
    <t>GTP-induced</t> fusion is bi-polarised. (A) S10s containing total MVs (MV0) were independently labelled with either BODIPY-C12 (donor) or diIC12 (acceptor) and mixed together. Sperm nuclei and ATP-GS (ATP) were added. Nuclear envelope remnants of the nuclei were pre-labelled with hydroxycoumarin. Epifluorescence patterns of labelled nuclei with bound MVs were <t>visualised</t> by phase contrast and two-photon fluorescence microscopy using a 100X objective. MVs were bound around the entire periphery of the nucleus. The nuclear envelope remnants mark the former apex and base of the sperm nucleus (white arrowheads). Fluorescence lifetime of BODIPY was measured before (t = 0) and after (t = 5, 15, 30, 45 and 60 minutes) the induction of NE formation by photo activation of caged-GTP. (B) Quantification of FRET FLIM images. For analyses, nuclei were divided in four quadrants: p1 and p2 correspond to the poles of the nuclei that include NER while e1 and e2 correspond to the equatorial regions. The averaged mean lifetime was for each quadrant was plotted for each time point showing that MVs fusion is initiated in the polar quadrants and propagates toward the equator. Errors bars correspond to the standard deviation from 7 independent experiments.
    Caged Gtp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caged gtp/product/Jena Bioscience
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caged gtp - by Bioz Stars, 2021-06
    85/100 stars
      Buy from Supplier

    Image Search Results


    Optimisation of the Click-PEGylation technique. (A) Effect of protein concentration on labelling efficiency during the Click-PEG reaction. Coomassie-stained mobility shift gels of purified GAPDH under untreated conditions reacted by Click-PEG red , comparing starting concentrations of 1 and 0.1 mg protein/mL. Profile plots of the ‘+ catalyst’ lanes were performed in FIJI. (B) Effect of propargyl-maleimide concentration on Click-PEG labelling. Coomassie-stained mobility shift gels of purified GAPDH reacted by Click-PEG red comparing 5 and 50 mM propargyl-maleimide, under untreated, reduced (10 mM TCEP) and oxidised (1 mM diamide) conditions. * indicates a higher molecular weight band. (C) Quantification of GAPDH thiol redox state distribution from (B). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means ±range of n=2 independent experiments. (D) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Coomassie-stained gel of purified GAPDH under reduced conditions (10 mM TCEP) reacted by Click-PEG red , comparing incubation times of 10, 30 and 120 min. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (E) Quantification of GAPDH thiol redox state distribution from (D). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments. (F) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Time course as for (D), except that GAPDH redox state was assessed by Western blotting. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (G) Quantification of GAPDH thiol redox state distribution from (F). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments.

    Journal: Free Radical Biology & Medicine

    Article Title: Click-PEGylation – A mobility shift approach to assess the redox state of cysteines in candidate proteins

    doi: 10.1016/j.freeradbiomed.2017.03.037

    Figure Lengend Snippet: Optimisation of the Click-PEGylation technique. (A) Effect of protein concentration on labelling efficiency during the Click-PEG reaction. Coomassie-stained mobility shift gels of purified GAPDH under untreated conditions reacted by Click-PEG red , comparing starting concentrations of 1 and 0.1 mg protein/mL. Profile plots of the ‘+ catalyst’ lanes were performed in FIJI. (B) Effect of propargyl-maleimide concentration on Click-PEG labelling. Coomassie-stained mobility shift gels of purified GAPDH reacted by Click-PEG red comparing 5 and 50 mM propargyl-maleimide, under untreated, reduced (10 mM TCEP) and oxidised (1 mM diamide) conditions. * indicates a higher molecular weight band. (C) Quantification of GAPDH thiol redox state distribution from (B). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means ±range of n=2 independent experiments. (D) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Coomassie-stained gel of purified GAPDH under reduced conditions (10 mM TCEP) reacted by Click-PEG red , comparing incubation times of 10, 30 and 120 min. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (E) Quantification of GAPDH thiol redox state distribution from (D). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments. (F) Effect of propargyl-maleimide incubation time on Click-PEG labelling. Time course as for (D), except that GAPDH redox state was assessed by Western blotting. Profile plots of the ‘–/+ catalyst’ lanes were performed in FIJI. (G) Quantification of GAPDH thiol redox state distribution from (F). Band densitometry was performed in FIJI and expressed as a % of total band intensity per lane. Data are means±range of n=2 independent experiments.

    Article Snippet: Samples were then reacted with 5 mM propargyl-maleimide at 37 °C for 30 min with agitation (1400 rpm), after which excess propargyl-maleimide was removed by passing samples through a spin column.

    Techniques: Protein Concentration, Staining, Mobility Shift, Purification, Concentration Assay, Molecular Weight, Incubation, Western Blot

    Click-PEGylation schemes. (A) Principle of the Click-PEGylation reaction. A reduced thiol is alkylated with propargyl-maleimide, then conjugated with an azide-PEG of high molecular weight (e.g. 5 kDa) using copper-catalysed Click chemistry. One of two possible regioisomers is depicted. (B) Click-PEG red reaction to label reduced thiols. A protein with two potentially reversibly oxidisable cysteine residues is shown. For Click-PEG red , the sample is reacted with propargyl-maleimide to label reduced cysteines, which are subsequently derivatised with azide-PEG via Click chemistry. Optionally, oxidised cysteines can then be reduced in vitro and blocked with NEM before separation by electrophoresis. (C) Click-PEG ox reaction to label oxidised thiols. Conversely, for ClickPEG ox , the sample is first reacted with NEM to block any reduced cysteine residues. Next, previously oxidised thiols are reduced in vitro, allowing their reaction with propargyl-maleimide and derivatisation with azide-PEG. Finally, samples are separated by electrophoresis to determine the resulting redox mobility shifts.

    Journal: Free Radical Biology & Medicine

    Article Title: Click-PEGylation – A mobility shift approach to assess the redox state of cysteines in candidate proteins

    doi: 10.1016/j.freeradbiomed.2017.03.037

    Figure Lengend Snippet: Click-PEGylation schemes. (A) Principle of the Click-PEGylation reaction. A reduced thiol is alkylated with propargyl-maleimide, then conjugated with an azide-PEG of high molecular weight (e.g. 5 kDa) using copper-catalysed Click chemistry. One of two possible regioisomers is depicted. (B) Click-PEG red reaction to label reduced thiols. A protein with two potentially reversibly oxidisable cysteine residues is shown. For Click-PEG red , the sample is reacted with propargyl-maleimide to label reduced cysteines, which are subsequently derivatised with azide-PEG via Click chemistry. Optionally, oxidised cysteines can then be reduced in vitro and blocked with NEM before separation by electrophoresis. (C) Click-PEG ox reaction to label oxidised thiols. Conversely, for ClickPEG ox , the sample is first reacted with NEM to block any reduced cysteine residues. Next, previously oxidised thiols are reduced in vitro, allowing their reaction with propargyl-maleimide and derivatisation with azide-PEG. Finally, samples are separated by electrophoresis to determine the resulting redox mobility shifts.

    Article Snippet: Samples were then reacted with 5 mM propargyl-maleimide at 37 °C for 30 min with agitation (1400 rpm), after which excess propargyl-maleimide was removed by passing samples through a spin column.

    Techniques: Molecular Weight, In Vitro, Electrophoresis, Blocking Assay

    GTP-induced fusion is bi-polarised. (A) S10s containing total MVs (MV0) were independently labelled with either BODIPY-C12 (donor) or diIC12 (acceptor) and mixed together. Sperm nuclei and ATP-GS (ATP) were added. Nuclear envelope remnants of the nuclei were pre-labelled with hydroxycoumarin. Epifluorescence patterns of labelled nuclei with bound MVs were visualised by phase contrast and two-photon fluorescence microscopy using a 100X objective. MVs were bound around the entire periphery of the nucleus. The nuclear envelope remnants mark the former apex and base of the sperm nucleus (white arrowheads). Fluorescence lifetime of BODIPY was measured before (t = 0) and after (t = 5, 15, 30, 45 and 60 minutes) the induction of NE formation by photo activation of caged-GTP. (B) Quantification of FRET FLIM images. For analyses, nuclei were divided in four quadrants: p1 and p2 correspond to the poles of the nuclei that include NER while e1 and e2 correspond to the equatorial regions. The averaged mean lifetime was for each quadrant was plotted for each time point showing that MVs fusion is initiated in the polar quadrants and propagates toward the equator. Errors bars correspond to the standard deviation from 7 independent experiments.

    Journal: PLoS ONE

    Article Title: Spatial Regulation of Membrane Fusion Controlled by Modification of Phosphoinositides

    doi: 10.1371/journal.pone.0012208

    Figure Lengend Snippet: GTP-induced fusion is bi-polarised. (A) S10s containing total MVs (MV0) were independently labelled with either BODIPY-C12 (donor) or diIC12 (acceptor) and mixed together. Sperm nuclei and ATP-GS (ATP) were added. Nuclear envelope remnants of the nuclei were pre-labelled with hydroxycoumarin. Epifluorescence patterns of labelled nuclei with bound MVs were visualised by phase contrast and two-photon fluorescence microscopy using a 100X objective. MVs were bound around the entire periphery of the nucleus. The nuclear envelope remnants mark the former apex and base of the sperm nucleus (white arrowheads). Fluorescence lifetime of BODIPY was measured before (t = 0) and after (t = 5, 15, 30, 45 and 60 minutes) the induction of NE formation by photo activation of caged-GTP. (B) Quantification of FRET FLIM images. For analyses, nuclei were divided in four quadrants: p1 and p2 correspond to the poles of the nuclei that include NER while e1 and e2 correspond to the equatorial regions. The averaged mean lifetime was for each quadrant was plotted for each time point showing that MVs fusion is initiated in the polar quadrants and propagates toward the equator. Errors bars correspond to the standard deviation from 7 independent experiments.

    Article Snippet: 3D Movie of nuclei visualised by FLIM at 15 minutes after photo-activation of caged GTP. (7.76 MB MOV) Click here for additional data file.

    Techniques: Fluorescence, Microscopy, Activation Assay, Standard Deviation

    3D view of nuclei visualised by FLIM. (A) Stack measurements of a nucleus: the first image corresponds to the fluorescence lifetime of the BODIPY measured at the top of a nucleus 15 minutes after photo-activation of caged GTP. Ten successive layers of the same nucleus were obtained. For each layer the focus of the objective was moved 0.25 µm along the Z-axis. Since the acquisition of one image lasts for 1 minute, the last image corresponding to the bottom of the nucleus was measured 25 minutes after the induction of NE formation. (B) 3D reconstructions from the Z-stacks of the same nucleus to form fluorescence lifetime 3D views. The indicated times correspond to the time elapsed after photo activation when the first image of each stack was measured.

    Journal: PLoS ONE

    Article Title: Spatial Regulation of Membrane Fusion Controlled by Modification of Phosphoinositides

    doi: 10.1371/journal.pone.0012208

    Figure Lengend Snippet: 3D view of nuclei visualised by FLIM. (A) Stack measurements of a nucleus: the first image corresponds to the fluorescence lifetime of the BODIPY measured at the top of a nucleus 15 minutes after photo-activation of caged GTP. Ten successive layers of the same nucleus were obtained. For each layer the focus of the objective was moved 0.25 µm along the Z-axis. Since the acquisition of one image lasts for 1 minute, the last image corresponding to the bottom of the nucleus was measured 25 minutes after the induction of NE formation. (B) 3D reconstructions from the Z-stacks of the same nucleus to form fluorescence lifetime 3D views. The indicated times correspond to the time elapsed after photo activation when the first image of each stack was measured.

    Article Snippet: 3D Movie of nuclei visualised by FLIM at 15 minutes after photo-activation of caged GTP. (7.76 MB MOV) Click here for additional data file.

    Techniques: Fluorescence, Activation Assay