cripto 1 Search Results


mouse anti hcr1 moab  (R&D Systems)
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R&D Systems mouse anti hcr1 moab
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recombinant soluble human cr1  (R&D Systems)
90
R&D Systems recombinant soluble human cr1
FIGURE 1. Characterization of the recom- binant <t>CR1</t> CCP 22–30_His fragment. (A) SDS-PAGE analysis of 4 mg CR1 CCP22-30 under reducing (R) and nonreducing (NR) conditions. The positions of the m.w. mark- ers are indicated. (B) CD spectroscopy of CR1 CCP22–30. A spectrum was recorded in the far-UV (200–260 nm) and collected six times. The mean values for each wavelength were calculated. The maximal ellipticity is indicated by an arrowhead. (C) Electron microscopy analysis of CR1 CCP22–30 (375000) after negative staining with 2% sodium silicotungstate.
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cripto  (Rockland Immunochemicals)
92
Rockland Immunochemicals cripto
FIGURE 1. Characterization of the recom- binant <t>CR1</t> CCP 22–30_His fragment. (A) SDS-PAGE analysis of 4 mg CR1 CCP22-30 under reducing (R) and nonreducing (NR) conditions. The positions of the m.w. mark- ers are indicated. (B) CD spectroscopy of CR1 CCP22–30. A spectrum was recorded in the far-UV (200–260 nm) and collected six times. The mean values for each wavelength were calculated. The maximal ellipticity is indicated by an arrowhead. (C) Electron microscopy analysis of CR1 CCP22–30 (375000) after negative staining with 2% sodium silicotungstate.
Cripto, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antibodies mabs  (R&D Systems)
91
R&D Systems antibodies mabs
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
Antibodies Mabs, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant human cripto  (R&D Systems)
90
R&D Systems recombinant human cripto
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
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goat anti human cripto 1  (R&D Systems)
90
R&D Systems goat anti human cripto 1
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
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human cripto 1  (R&D Systems)
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R&D Systems human cripto 1
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
Human Cripto 1, supplied by R&D Systems, 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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human cripto 1 duoset elisa development kit  (R&D Systems)
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R&D Systems human cripto 1 duoset elisa development kit
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
Human Cripto 1 Duoset Elisa Development Kit, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cfc1/cripto-1 blocking peptide cripto-1  (GeneTex)
90
GeneTex cfc1/cripto-1 blocking peptide cripto-1
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
Cfc1/Cripto 1 Blocking Peptide Cripto 1, supplied by GeneTex, 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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recombinant cripto-1 protein  (Promega)
90
Promega recombinant cripto-1 protein
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
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monoclonal antibodies against cleaved, purified cripto-1  (ABclonal Biotechnology)
90
ABclonal Biotechnology monoclonal antibodies against cleaved, purified cripto-1
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
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high-affinity antibodies against distinct cripto-1 domains  (ABclonal Biotechnology)
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ABclonal Biotechnology high-affinity antibodies against distinct cripto-1 domains
FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 <t>mAb</t> (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.
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Image Search Results


FIGURE 1. Characterization of the recom- binant CR1 CCP 22–30_His fragment. (A) SDS-PAGE analysis of 4 mg CR1 CCP22-30 under reducing (R) and nonreducing (NR) conditions. The positions of the m.w. mark- ers are indicated. (B) CD spectroscopy of CR1 CCP22–30. A spectrum was recorded in the far-UV (200–260 nm) and collected six times. The mean values for each wavelength were calculated. The maximal ellipticity is indicated by an arrowhead. (C) Electron microscopy analysis of CR1 CCP22–30 (375000) after negative staining with 2% sodium silicotungstate.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Deciphering complement receptor type 1 interactions with recognition proteins of the lectin complement pathway.

doi: 10.4049/jimmunol.1202451

Figure Lengend Snippet: FIGURE 1. Characterization of the recom- binant CR1 CCP 22–30_His fragment. (A) SDS-PAGE analysis of 4 mg CR1 CCP22-30 under reducing (R) and nonreducing (NR) conditions. The positions of the m.w. mark- ers are indicated. (B) CD spectroscopy of CR1 CCP22–30. A spectrum was recorded in the far-UV (200–260 nm) and collected six times. The mean values for each wavelength were calculated. The maximal ellipticity is indicated by an arrowhead. (C) Electron microscopy analysis of CR1 CCP22–30 (375000) after negative staining with 2% sodium silicotungstate.

Article Snippet: Recombinant soluble human CR1 was purchased from R&D Systems Europe (Lille, France).

Techniques: SDS Page, Circular Dichroism, Electron Microscopy, Negative Staining

FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 mAb (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.

Journal: Journal of Biological Chemistry

Article Title: Growth Factor Induction of Cripto-1 Shedding by Glycosylphosphatidylinositol-Phospholipase D and Enhancement of Endothelial Cell Migration

doi: 10.1074/jbc.m702713200

Figure Lengend Snippet: FIGURE 1. Lipid raft localization and release of CR-1 protein. A, NTERA2/D1 cells were stained with anti-CR-1 mAb (green), and lipid raft marker GM-1 was labeled with CTxB (red) without permeabilization and analyzed by confocal microscopy (upper panel). Magnified images for the marked regions in the upper panel are shown in the lower left panel. Negative controls without pri- mary antibody are shown in the lower right panel. Nuclei were stained with DAPI (blue) in all merged images. Scale bar 10 m. B, biochemical isolation of DRMs with 1% Triton X-100 by sucrose-gradient centrifugation of NTERA2/D1 cells. The gradient fractions (lanes 4–12) were analyzed with Western blot analysis for CR-1. Transferrin receptor (TfR) was used as a control for non-raft membrane protein. The lipid raft marker GM-1 in the same sam- ples was detected with HRP-conjugated CTxB by dot-blot analysis. C, compar- ative study of cell-associated (CL) and released (CM) CR-1 with or without serum by semi-quantitative Western blot analysis (see Table 1 and supple- mental Fig. S1, A–C). A representative blot for NTERA2/D1 cells is shown. The indicated amount of recombinant human CR-1 protein was used as a standard.

Article Snippet: Reagents—Human CR-1 monoclonal antibodies (mAbs) (MAB2771 and FAB2772P) were obtained from R&D Systems (Minneapolis, MN) or developed as previously reported (B3F6) (8).

Techniques: Staining, Marker, Labeling, Confocal Microscopy, Isolation, Gradient Centrifugation, Western Blot, Control, Membrane, Dot Blot, Recombinant