mouse albumin Search Results


大鼠尾动脉压及尿蛋白检测 造模前1 d及实验期间每周通过无创小鼠尾动脉血压测量仪  (Assaypro)
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Assaypro 大鼠尾动脉压及尿蛋白检测 造模前1 d及实验期间每周通过无创小鼠尾动脉血压测量仪
大鼠尾动脉压及尿蛋白检测 造模前1 D及实验期间每周通过无创小鼠尾动脉血压测量仪, supplied by Assaypro, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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大鼠尾动脉压及尿蛋白检测 造模前1 d及实验期间每周通过无创小鼠尾动脉血压测量仪 - by Bioz Stars, 2026-02
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mouse monoclonal antibody  (TaKaRa)
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TaKaRa mouse monoclonal antibody
FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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ovalbumin proteins  (Valiant Co Ltd)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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mouse albumin enzyme  (Bethyl)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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immunosorbent assay elisa kit  (ALPCO)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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resource source identifier antibodies goat anti mouse albumin antibody bethyl laboratories a90 134a hnf 4a antibody  (Bethyl)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
Resource Source Identifier Antibodies Goat Anti Mouse Albumin Antibody Bethyl Laboratories A90 134a Hnf 4a Antibody, supplied by Bethyl, 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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room temperature  (Bio-Rad)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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mouse serum  (Cusabio)
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Cusabio mouse serum
FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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mouse serum albumin  (Equitech-Bio inc)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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anti albumin antibody  (R&D Systems)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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anti human alb polyclonal antibody goat bethyl laboratories a90 234b  (Bethyl)
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FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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albumin  (Bio-Rad)
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Bio-Rad albumin
FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a <t>monoclonal</t> antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.
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Image Search Results


FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a monoclonal antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.

Journal: The Journal of biological chemistry

Article Title: Protein stability and domain topology determine the transcriptional activity of the mammalian glial cells missing homolog, GCMb.

doi: 10.1074/jbc.275.7.4774

Figure Lengend Snippet: FIG. 3. Transcriptional activities of the two mammalian GCM homologs. A, expression of mGCMa and mGCMb proteins in transfected cells was confirmed by Western blot analyses of COS nuclear extracts using a polyclonal antiserum against mGCMa and a monoclonal antibody directed against the T7-epitope tag on mGCMb, respectively. Numbers indicate size of molecular mass markers in kDa. B–E, a luciferase reporter plasmid carrying six tandemly arranged GCM binding sites (6x gbs luc) was transfected into U138 glioblastoma cells (B), COS cells (C), 293 cells (D), and Drosophila S2 cells (E) together with standard amounts (2 mg) of empty expression plasmid (2) or expression plasmids for mGCMa or mGCMb. Luciferase activities in extracts from transfected cells were determined in three independent experiments each performed in duplicates. Data are presented as fold inductions that were calculated for each reporter plasmid by comparing luciferase activities to values from cells transfected with reporter plasmid and empty expression plasmid. F, 6x gbs luc was transfected in 293 cells with increasing amounts of expression plasmids for epitope-tagged mGCMa or mGCMb (5 ng, 50 ng, 500 ng, 2 mg, 4 mg). The amounts of epitope-tagged mGCMa and mGCMb present in transfected 293 cells were determined by Western blot analysis using a monoclonal antibody directed against the T7 epitope (G). Equal amounts of extracts were used in each lane. All lanes were developed simultaneously and for the same length of time. The asterisks mark a cross-reactive band present in 293 extracts.

Article Snippet: The following primary antibodies were used: a polyclonal rabbit antiserum directed against amino acids 169–436 of mGCMa, a polyclonal rabbit antiserum directed against the POU domain of Tst-1/Oct6/SCIP, a purified mouse monoclonal antibody directed against the T7 tag epitope (Novagen), and a purified mouse monoclonal antibody directed against the Gal4 DNAbinding domain (CLONTECH).

Techniques: Expressing, Transfection, Western Blot, Luciferase, Plasmid Preparation, Binding Assay

FIG. 5. Fusion proteins between regions of mGCMb and the DNA-binding domain of Gal4. A, summary of Gal4 DNA-binding domain (Gal4 DBD) constructs. The mGCMb regions present in each fusion protein are indicated by the first and last amino acid still con- tained within the fragment. Gal4(aC) represents a fusion between Gal4 DBD and amino acids 169–436 of mGCMa. Gal4(aTA2) contains amino acids 330–436 of mGCMa fused to Gal4 DBD (13). B, the Gal4-respon- sive luciferase reporter (3x UAS luc) was transfected into 293 cells together with expression plasmids for Gal4 DBD or for the Gal4 DBD fusions depicted in A. Luciferase activities were determined in three independent experiments, each performed in duplicate. Data are pre- sented for each Gal4 DBD fusion as fold induction above the level of luciferase activity obtained in transfections with an expression plasmid for Gal4 DBD alone, which was given an arbitrary value of 1. C, expression of Gal4 DBD fusion proteins was analyzed by Western blots of nuclear extracts from transfected 293 cells with a monoclonal anti- body against the Gal4 DBD. Numbers indicate size of molecular mass markers in kDa.

Journal: The Journal of biological chemistry

Article Title: Protein stability and domain topology determine the transcriptional activity of the mammalian glial cells missing homolog, GCMb.

doi: 10.1074/jbc.275.7.4774

Figure Lengend Snippet: FIG. 5. Fusion proteins between regions of mGCMb and the DNA-binding domain of Gal4. A, summary of Gal4 DNA-binding domain (Gal4 DBD) constructs. The mGCMb regions present in each fusion protein are indicated by the first and last amino acid still con- tained within the fragment. Gal4(aC) represents a fusion between Gal4 DBD and amino acids 169–436 of mGCMa. Gal4(aTA2) contains amino acids 330–436 of mGCMa fused to Gal4 DBD (13). B, the Gal4-respon- sive luciferase reporter (3x UAS luc) was transfected into 293 cells together with expression plasmids for Gal4 DBD or for the Gal4 DBD fusions depicted in A. Luciferase activities were determined in three independent experiments, each performed in duplicate. Data are pre- sented for each Gal4 DBD fusion as fold induction above the level of luciferase activity obtained in transfections with an expression plasmid for Gal4 DBD alone, which was given an arbitrary value of 1. C, expression of Gal4 DBD fusion proteins was analyzed by Western blots of nuclear extracts from transfected 293 cells with a monoclonal anti- body against the Gal4 DBD. Numbers indicate size of molecular mass markers in kDa.

Article Snippet: The following primary antibodies were used: a polyclonal rabbit antiserum directed against amino acids 169–436 of mGCMa, a polyclonal rabbit antiserum directed against the POU domain of Tst-1/Oct6/SCIP, a purified mouse monoclonal antibody directed against the T7 tag epitope (Novagen), and a purified mouse monoclonal antibody directed against the Gal4 DNAbinding domain (CLONTECH).

Techniques: Binding Assay, Construct, Luciferase, Transfection, Expressing, Activity Assay, Plasmid Preparation, Western Blot