lukf pv egfp fusion protein Search Results


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GE Healthcare gst lukf pv fusion proteins
Biological activity of <t>GST</t> fusion proteins. (a) Control of homogeneity by 3%–8% (w/vol) SDS-PAGE of 200 ng of each purified protein is shown; (1) molecular ladder, (2) <t>LukF-PV,</t> (3) GST∼LukF-PV, (4) LukS-PV, (5) GST∼LukS-PV. (b) Flow cytometry evaluation of the Ca 2+ entry into human PMNs mediated by combinations of wild-type LukS-PV and LukF-PV and GST fusion proteins. (c) Flow cytometry evaluation of the ethidium entry into human PMNs mediated by combinations of LukS-PV and LukF-PV and GST fusion proteins. (d) Hydrodynamic radius of pores formed by WT and fusion proteins in human PMNs determined after a 30-minute incubation of toxins (20 nM of S and 100 nM of F components). Osmotic protection by polyethylene glycol molecules was assessed by variations of the mean FSC (forward light scatter) value in the presence of PEG molecules of different hydrodynamic radii.
Gst Lukf Pv Fusion Proteins, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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PROTEINA Co Ltd proteina proteinb
Biological activity of <t>GST</t> fusion proteins. (a) Control of homogeneity by 3%–8% (w/vol) SDS-PAGE of 200 ng of each purified protein is shown; (1) molecular ladder, (2) <t>LukF-PV,</t> (3) GST∼LukF-PV, (4) LukS-PV, (5) GST∼LukS-PV. (b) Flow cytometry evaluation of the Ca 2+ entry into human PMNs mediated by combinations of wild-type LukS-PV and LukF-PV and GST fusion proteins. (c) Flow cytometry evaluation of the ethidium entry into human PMNs mediated by combinations of LukS-PV and LukF-PV and GST fusion proteins. (d) Hydrodynamic radius of pores formed by WT and fusion proteins in human PMNs determined after a 30-minute incubation of toxins (20 nM of S and 100 nM of F components). Osmotic protection by polyethylene glycol molecules was assessed by variations of the mean FSC (forward light scatter) value in the presence of PEG molecules of different hydrodynamic radii.
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PROTEINA Co Ltd dimer proteina/protein
Biological activity of <t>GST</t> fusion proteins. (a) Control of homogeneity by 3%–8% (w/vol) SDS-PAGE of 200 ng of each purified protein is shown; (1) molecular ladder, (2) <t>LukF-PV,</t> (3) GST∼LukF-PV, (4) LukS-PV, (5) GST∼LukS-PV. (b) Flow cytometry evaluation of the Ca 2+ entry into human PMNs mediated by combinations of wild-type LukS-PV and LukF-PV and GST fusion proteins. (c) Flow cytometry evaluation of the ethidium entry into human PMNs mediated by combinations of LukS-PV and LukF-PV and GST fusion proteins. (d) Hydrodynamic radius of pores formed by WT and fusion proteins in human PMNs determined after a 30-minute incubation of toxins (20 nM of S and 100 nM of F components). Osmotic protection by polyethylene glycol molecules was assessed by variations of the mean FSC (forward light scatter) value in the presence of PEG molecules of different hydrodynamic radii.
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Image Search Results


Biological activity of GST fusion proteins. (a) Control of homogeneity by 3%–8% (w/vol) SDS-PAGE of 200 ng of each purified protein is shown; (1) molecular ladder, (2) LukF-PV, (3) GST∼LukF-PV, (4) LukS-PV, (5) GST∼LukS-PV. (b) Flow cytometry evaluation of the Ca 2+ entry into human PMNs mediated by combinations of wild-type LukS-PV and LukF-PV and GST fusion proteins. (c) Flow cytometry evaluation of the ethidium entry into human PMNs mediated by combinations of LukS-PV and LukF-PV and GST fusion proteins. (d) Hydrodynamic radius of pores formed by WT and fusion proteins in human PMNs determined after a 30-minute incubation of toxins (20 nM of S and 100 nM of F components). Osmotic protection by polyethylene glycol molecules was assessed by variations of the mean FSC (forward light scatter) value in the presence of PEG molecules of different hydrodynamic radii.

Journal: Journal of Biomedicine and Biotechnology

Article Title: Distinction between Pore Assembly by Staphylococcal α -Toxin versus Leukotoxins

doi: 10.1155/2007/25935

Figure Lengend Snippet: Biological activity of GST fusion proteins. (a) Control of homogeneity by 3%–8% (w/vol) SDS-PAGE of 200 ng of each purified protein is shown; (1) molecular ladder, (2) LukF-PV, (3) GST∼LukF-PV, (4) LukS-PV, (5) GST∼LukS-PV. (b) Flow cytometry evaluation of the Ca 2+ entry into human PMNs mediated by combinations of wild-type LukS-PV and LukF-PV and GST fusion proteins. (c) Flow cytometry evaluation of the ethidium entry into human PMNs mediated by combinations of LukS-PV and LukF-PV and GST fusion proteins. (d) Hydrodynamic radius of pores formed by WT and fusion proteins in human PMNs determined after a 30-minute incubation of toxins (20 nM of S and 100 nM of F components). Osmotic protection by polyethylene glycol molecules was assessed by variations of the mean FSC (forward light scatter) value in the presence of PEG molecules of different hydrodynamic radii.

Article Snippet: GST∼LukS-PV and GST∼LukF-PV fusion proteins were purified for functional analysis by chromatography on glutathione-sepharose 4B followed by hydrophobic interaction chromatography (HIC, alkyl-superose, i.e., resource ISO—Ge Healthcare, USA).

Techniques: Activity Assay, SDS Page, Purification, Flow Cytometry, Incubation

Oligomers formed by PVL and modified toxins. Oligomers were checked in solution or after recovery from treated human PMNs, 3–8% (w/v) SDS-PAGE and immunoblotting with anti-LukS-PV and anti-LukF-PV affinity-purified rabbit antibodies. Lane 1: LukS-PV + LukF-PV without membranes, lane 2: PMNs only, lane 3: GST∼LukS-PV + GST∼LukF-PV, lanes 4, 5, 6: toxins applied on PMNs membranes and then saponin/glutaraldehyde treated and heated 5 minutes at 100°C as described in materials and methods, lane 4: LukS-PV + GST∼LukF-PV, lane 5: GST∼LukS-PV + LukF-PV, lane 6: GST∼LukS-PV + GST∼LukF-PV.

Journal: Journal of Biomedicine and Biotechnology

Article Title: Distinction between Pore Assembly by Staphylococcal α -Toxin versus Leukotoxins

doi: 10.1155/2007/25935

Figure Lengend Snippet: Oligomers formed by PVL and modified toxins. Oligomers were checked in solution or after recovery from treated human PMNs, 3–8% (w/v) SDS-PAGE and immunoblotting with anti-LukS-PV and anti-LukF-PV affinity-purified rabbit antibodies. Lane 1: LukS-PV + LukF-PV without membranes, lane 2: PMNs only, lane 3: GST∼LukS-PV + GST∼LukF-PV, lanes 4, 5, 6: toxins applied on PMNs membranes and then saponin/glutaraldehyde treated and heated 5 minutes at 100°C as described in materials and methods, lane 4: LukS-PV + GST∼LukF-PV, lane 5: GST∼LukS-PV + LukF-PV, lane 6: GST∼LukS-PV + GST∼LukF-PV.

Article Snippet: GST∼LukS-PV and GST∼LukF-PV fusion proteins were purified for functional analysis by chromatography on glutathione-sepharose 4B followed by hydrophobic interaction chromatography (HIC, alkyl-superose, i.e., resource ISO—Ge Healthcare, USA).

Techniques: Modification, SDS Page, Western Blot, Affinity Purification