vsvg antibody Search Results


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Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, <t>and</t> <t>MMP14</t> is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, <t>VSVG-SBP</t> – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.
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Institut Curie anti-vsvg antibody
Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, <t>and</t> <t>MMP14</t> is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, <t>VSVG-SBP</t> – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.
Anti Vsvg Antibody, supplied by Institut Curie, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Covance rabbit antibody against vsvg
Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, <t>and</t> <t>MMP14</t> is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, <t>VSVG-SBP</t> – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.
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Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, <t>and</t> <t>MMP14</t> is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, <t>VSVG-SBP</t> – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.
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Amersham Pharmacia Biotech Ltd polyclonal anti-vsvg antibodies
Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, <t>and</t> <t>MMP14</t> is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, <t>VSVG-SBP</t> – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.
Polyclonal Anti Vsvg Antibodies, supplied by Amersham Pharmacia Biotech Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, and MMP14 is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, VSVG-SBP – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.

Journal: The Journal of Cell Biology

Article Title: GRAF2, WDR44, and MICAL1 mediate Rab8/10/11–dependent export of E-cadherin, MMP14, and CFTR ΔF508

doi: 10.1083/jcb.201811014

Figure Lengend Snippet: Export of neosynthesized CFTR, CFTR ΔF508, E-cadherin, and MMP14 is sensitive to ER stress. (A) Export efficiency of GFP – Extope CFTR or GFP – Extope CFTR ΔF508 in 293T cells, of E-cadherin – RFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells and of MMP14-GFP in HT 1080 cells. n = 3 – 6. Sar1 H79G increased export of GFP – Extope CFTR ΔF508 but inhibited export of E-cadherin – RFP and MMP14-GFP. (B) Export efficiency of GFP – Extope CFTR ΔF508 in 293T cells and of E-cadherin – GFP, MMP14-GFP, HA – α 2B -AR – RFP, or GFP-GPI in HeLa cells. For GFP – Extope CFTR ΔF508, cells were left untreated, incubated with BFA (1.25 µg/ml, 12 h), or thapsigargin (1 µM, 2 h), the latter followed by a 2-h chase . Cells were collected 36 h after transfection. HeLa cells were incubated with BFA (1.25 µg/ml, 6 h) or thapsigargin (1 µM, 6 h) and collected 12 h after transfection. Basal and ER stress-induced export of GFP – Extope CFTR ΔF508 was inhibited by RFP – Rab10 T23N. ER stress inhibited export of E-cadherin – GFP and MMP14-GFP. n = 4 – 6. (A and B) The dashed line represents the export efficiency under control conditions. (C) Biotinylation of surface proteins in transfected 293T cells. Export efficiency of GFP – CFTR ΔF508 was quantified using single-transfected cells (left) or cells cotransfected with myc – Sar1 H79G (right) as control. n = 3 – 5. The Transferrin receptor (TfnR) was used as loading control. In each case, the two parts of the blots are from the same membrane and correspond to identical exposure times. (D) Schematic representation of the RUSH proteins used. (E and F) Transfected HeLa cells were left untreated or incubated with biotin (40 µM, 1 h). (E) Export efficiency of RUSH proteins. n = 3 – 5. (A, B, C, and E) Data are means ± SEM; *, P < 0.05; **, P < 0.01; ***, P < 0.001; and ****, P < 0.0001. (F) Confocal images after staining with DyLight 650 α-HA. In untreated cells, VSVG-SBP – Fusion Red was in the ER where it colocalized with the Streptavidin-HA-Ii retention hook; E-cadherin – SBP-GFP did not accumulate in the ER and was already found at the plasma membrane. Upon biotin addition, VSVG-SBP-GFP was released from the ER and translocated to the plasma membrane. Insets show magnifications of the boxed areas. Scale bars: 10 µm; scale bars of insets: 4 µm.

Article Snippet: Hildreth); ERGIC53 (mouse, clone G1/93, Cat# 804–602, RRID:AB_2234610; Alexis Biochemicals); MICAL-L1 (mouse, Cat# H00085377-B01P, RRID:AB_2143767; Novus Biologicals); Grp78 (mouse, clone 40/BiP, Cat# 610978, RRID:AB_398291; BD Biosciences); E-cadherin (rat, clone ECCD-2, Cat# 13–1900, RRID:AB_2533005; Thermo Fisher Scientific); MMP14 (rabbit, Cat# ab3644, RRID:AB_303973; Abcam); VSVG (mouse, clone 8G5F11, Cat# EB0010, RRID:AB_2811223; Kerafast); β-tubulin (mouse, clone 2–28-33, Cat# T5293, RRID:AB_477580; Sigma); Actin (mouse, clone AC-15, Cat# ab6276, RRID:AB_2223210; Abcam); Integrin-β1 (mouse, clone TS2/16, Cat# LS-C106376, RRID:AB_10626118; LifeSpan Biosciences); Alexa Fluor 647 Integrin-β1 (mouse, clone TS2/16, Cat# 303018, RRID:AB_2130080; BioLegend); Alexa Fluor 647 GFP (rabbit, Cat# A-31852, RRID:AB_162553; Thermo Fisher Scientific); and DyLight 650 conjugated HA (mouse, clone 16B12, Cat# ab117515, RRID:AB_10999718; Abcam).

Techniques: Incubation, Transfection, Staining