s2 cells Search Results


s2 cells  (Expression Systems Inc)
99
Expression Systems Inc s2 cells
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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nα fmoc nω  (Chem Impex International)
95
Chem Impex International nα fmoc nω
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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glutathione gsh  (Chem Impex International)
95
Chem Impex International glutathione gsh
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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a15140  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc a15140
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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pro caspase 8  (Cell Signaling Technology Inc)
86
Cell Signaling Technology Inc pro caspase 8
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
Pro Caspase 8, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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крысы 4 й группы получали вкхдр с добавлением ala  (Chem Impex International)
95
Chem Impex International крысы 4 й группы получали вкхдр с добавлением ala
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
крысы 4 й группы получали вкхдр с добавлением Ala, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibody against sars cov 2 spike protein s2  (Cell Signaling Technology Inc)
92
Cell Signaling Technology Inc antibody against sars cov 2 spike protein s2
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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o t butyl l tyrosine t butyl ester hydrochloride  (Chem Impex International)
95
Chem Impex International o t butyl l tyrosine t butyl ester hydrochloride
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
O T Butyl L Tyrosine T Butyl Ester Hydrochloride, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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situ heating system  (DENSsolutions)
96
DENSsolutions situ heating system
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
Situ Heating System, supplied by DENSsolutions, 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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linker 4 formylphenyl sulfonyl l isoleucine  (Chem Impex International)
95
Chem Impex International linker 4 formylphenyl sulfonyl l isoleucine
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
Linker 4 Formylphenyl Sulfonyl L Isoleucine, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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na fmoc n im trityl l histidine  (Chem Impex International)
95
Chem Impex International na fmoc n im trityl l histidine
FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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fmoc β amino acids  (Chem Impex International)
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FIG. 2. Subcellular localization and purification of <t>D.</t> <t>SiaT</t> protein. A, immunofluorescent staining of Drosophila <t>S2</t> cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.
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Image Search Results


FIG. 2. Subcellular localization and purification of D. SiaT protein. A, immunofluorescent staining of Drosophila S2 cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.

Journal: Journal of Biological Chemistry

Article Title: Functional Characterization of Drosophila Sialyltransferase

doi: 10.1074/jbc.m309912200

Figure Lengend Snippet: FIG. 2. Subcellular localization and purification of D. SiaT protein. A, immunofluorescent staining of Drosophila S2 cells expressing D. SiaT-HA protein reveals its co-localization with Golgi resident protein (Lva): red (Cy3), D. SiaT; green (FITC), Lva. Right panel shows the overlay of red and green channels. B, Western blot analysis with anti-HA antibody revealed the presence of D. SiaT-HA protein in the cell medium and cell pellet fractions of transiently transfected Drosophila S2 culture cells. C, Western blot and Coomassie staining of purified protein A-tagged D. SiaT protein. Protein A-SiaT fusion protein was expressed in Sf9 cells using baculovirus system, purified using Sepharose-IgG beads, separated on SDS-PAGE gel, and analyzed by Western blotting (probed with purified rabbit IgG) and Coomassie staining. Beads from mock purification (Sf9 cells infected with irrelevant baculovirus) were used as a negative control. Based on Coomassie staining, the purity of IgG-immobilized D. SiaT protein was estimated to be 98%.

Article Snippet: As larger D. SiaT quantities than could be conveniently produced in S2 cells were required for comprehensive enzymatic characterization, D. SiaT recombinant protein was also expressed in Sf9 cells using the baculovirus expression system (Invitrogen).

Techniques: Purification, Staining, Expressing, Western Blot, Transfection, SDS Page, Infection, Negative Control