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Qiagen the mircury lna array (version 18.0) station
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Bio-Rad kilodaltons
SDS-PAGE gel autoradiograph demonstrating an 85-kDa surface protein (arrow) in 125I-labeled Caco-2 cells (lane 1) bound by CSL and immunoprecipitated by MAb 3E2 (lane 2). 125I-labeled RSE-1 cell surface proteins before (lane 4) and after (lane 5) incubation with CSL and precipitation with MAb 3E2 are shown for comparison. Lanes 3 and 6 were loaded with isotype control MAb-CSL precipitates from 125I-labeled Caco-2 or RSE-1 cells, respectively. Molecular mass standards are indicated on the left in <t>kilodaltons</t> (myosin, 200 kDa; β-galactosidase, 97.4 kDa; BSA, 69 kDa; ovalbumin, 46 kDa; carbonic anhydrase, 30 kDa; and trypsin inhibitor, 21.5 kDa) (Amersham Pharmacia Biotech).
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GraphPad Software Inc graphpad prism v8
SDS-PAGE gel autoradiograph demonstrating an 85-kDa surface protein (arrow) in 125I-labeled Caco-2 cells (lane 1) bound by CSL and immunoprecipitated by MAb 3E2 (lane 2). 125I-labeled RSE-1 cell surface proteins before (lane 4) and after (lane 5) incubation with CSL and precipitation with MAb 3E2 are shown for comparison. Lanes 3 and 6 were loaded with isotype control MAb-CSL precipitates from 125I-labeled Caco-2 or RSE-1 cells, respectively. Molecular mass standards are indicated on the left in <t>kilodaltons</t> (myosin, 200 kDa; β-galactosidase, 97.4 kDa; BSA, 69 kDa; ovalbumin, 46 kDa; carbonic anhydrase, 30 kDa; and trypsin inhibitor, 21.5 kDa) (Amersham Pharmacia Biotech).
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Image Search Results


SDS-PAGE gel autoradiograph demonstrating an 85-kDa surface protein (arrow) in 125I-labeled Caco-2 cells (lane 1) bound by CSL and immunoprecipitated by MAb 3E2 (lane 2). 125I-labeled RSE-1 cell surface proteins before (lane 4) and after (lane 5) incubation with CSL and precipitation with MAb 3E2 are shown for comparison. Lanes 3 and 6 were loaded with isotype control MAb-CSL precipitates from 125I-labeled Caco-2 or RSE-1 cells, respectively. Molecular mass standards are indicated on the left in kilodaltons (myosin, 200 kDa; β-galactosidase, 97.4 kDa; BSA, 69 kDa; ovalbumin, 46 kDa; carbonic anhydrase, 30 kDa; and trypsin inhibitor, 21.5 kDa) (Amersham Pharmacia Biotech).

Journal:

Article Title: Characterization of an Intestinal Epithelial Cell Receptor Recognized by the Cryptosporidium parvum Sporozoite Ligand CSL

doi: 10.1128/IAI.69.3.1661-1670.2001

Figure Lengend Snippet: SDS-PAGE gel autoradiograph demonstrating an 85-kDa surface protein (arrow) in 125I-labeled Caco-2 cells (lane 1) bound by CSL and immunoprecipitated by MAb 3E2 (lane 2). 125I-labeled RSE-1 cell surface proteins before (lane 4) and after (lane 5) incubation with CSL and precipitation with MAb 3E2 are shown for comparison. Lanes 3 and 6 were loaded with isotype control MAb-CSL precipitates from 125I-labeled Caco-2 or RSE-1 cells, respectively. Molecular mass standards are indicated on the left in kilodaltons (myosin, 200 kDa; β-galactosidase, 97.4 kDa; BSA, 69 kDa; ovalbumin, 46 kDa; carbonic anhydrase, 30 kDa; and trypsin inhibitor, 21.5 kDa) (Amersham Pharmacia Biotech).

Article Snippet: Molecular mass standards (Bio-Rad, Hercules, Calif.) are indicated on the left in kilodaltons (myosin, 208 kDa; β-galactosidase, 127 kDa; BSA, 85 kDa; carbonic anhydrase, 45 kDa; soybean trypsin inhibitor, 32.8 kDa; lysozyme, 18.1 kDa; and aprotinin, 7.4 kDa). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window FIG. 6 caption a7 Dot immunoblot demonstrating specific binding of CSL to CSL-R following isolation from Caco-2 cells.

Techniques: SDS Page, Autoradiography, Labeling, Immunoprecipitation, Incubation

Silver-stained SDS-polyacrylamide gel demonstrating an 85-kDa protein (arrow) in Caco-2 cells (lane 1, 4.0 μg) isolated by CSL affinity chromatography (lane 2, 0.3 μg). Lane 3 was loaded with sample buffer to identify silver stain artifacts. Molecular mass standards (Bio-Rad, Hercules, Calif.) are indicated on the left in kilodaltons (myosin, 208 kDa; β-galactosidase, 127 kDa; BSA, 85 kDa; carbonic anhydrase, 45 kDa; soybean trypsin inhibitor, 32.8 kDa; lysozyme, 18.1 kDa; and aprotinin, 7.4 kDa).

Journal:

Article Title: Characterization of an Intestinal Epithelial Cell Receptor Recognized by the Cryptosporidium parvum Sporozoite Ligand CSL

doi: 10.1128/IAI.69.3.1661-1670.2001

Figure Lengend Snippet: Silver-stained SDS-polyacrylamide gel demonstrating an 85-kDa protein (arrow) in Caco-2 cells (lane 1, 4.0 μg) isolated by CSL affinity chromatography (lane 2, 0.3 μg). Lane 3 was loaded with sample buffer to identify silver stain artifacts. Molecular mass standards (Bio-Rad, Hercules, Calif.) are indicated on the left in kilodaltons (myosin, 208 kDa; β-galactosidase, 127 kDa; BSA, 85 kDa; carbonic anhydrase, 45 kDa; soybean trypsin inhibitor, 32.8 kDa; lysozyme, 18.1 kDa; and aprotinin, 7.4 kDa).

Article Snippet: Molecular mass standards (Bio-Rad, Hercules, Calif.) are indicated on the left in kilodaltons (myosin, 208 kDa; β-galactosidase, 127 kDa; BSA, 85 kDa; carbonic anhydrase, 45 kDa; soybean trypsin inhibitor, 32.8 kDa; lysozyme, 18.1 kDa; and aprotinin, 7.4 kDa). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window FIG. 6 caption a7 Dot immunoblot demonstrating specific binding of CSL to CSL-R following isolation from Caco-2 cells.

Techniques: Staining, Isolation, Affinity Chromatography, Silver Staining